GenomeNet

Database: UniProt
Entry: P48633
LinkDB: P48633
Original site: P48633 
ID   HMWP2_YERE8             Reviewed;        2035 AA.
AC   P48633; A1JTF8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-NOV-2024, entry version 142.
DE   RecName: Full=High-molecular-weight protein 2;
DE            Short=HMWP2;
GN   Name=irp2; OrderedLocusNames=YE2617;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8366034; DOI=10.1128/jb.175.17.5488-5504.1993;
RA   Guilvout I., Mercereau-Puijalon O., Bonnefoy S., Pugsley A.P., Carniel E.;
RT   "High-molecular-weight protein 2 of Yersinia enterocolitica is homologous
RT   to AngR of Vibrio anguillarum and belongs to a family of proteins involved
RT   in nonribosomal peptide synthesis.";
RL   J. Bacteriol. 175:5488-5504(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Unknown. May be involved in the nonribosomal synthesis of
CC       small peptides.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000305};
CC       Note=Binds 3 phosphopantetheines covalently. {ECO:0000305};
CC   -!- DOMAIN: Consists of a central region with similarity to the repeat
CC       domains of ACVS and GRC2, flanked by two repeat domains, each of which
CC       contains 5 direct repeats.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L18881; AAA27636.1; -; Genomic_DNA.
DR   EMBL; Z35454; CAA84606.1; -; Genomic_DNA.
DR   EMBL; AM286415; CAL12654.1; -; Genomic_DNA.
DR   PIR; A48654; A48654.
DR   RefSeq; WP_011816641.1; NC_008800.1.
DR   RefSeq; YP_001006815.1; NC_008800.1.
DR   AlphaFoldDB; P48633; -.
DR   SMR; P48633; -.
DR   KEGG; yen:YE2617; -.
DR   PATRIC; fig|393305.7.peg.2780; -.
DR   eggNOG; COG1020; Bacteria.
DR   eggNOG; COG2226; Bacteria.
DR   eggNOG; COG3433; Bacteria.
DR   HOGENOM; CLU_000022_40_0_6; -.
DR   OrthoDB; 9757559at2; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0009366; C:enterobactin synthetase complex; IEA:TreeGrafter.
DR   GO; GO:0047527; F:2,3-dihydroxybenzoate-serine ligase activity; IEA:TreeGrafter.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0009239; P:enterobactin biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR   CDD; cd12114; A_NRPS_TlmIV_like; 1.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd19535; Cyc_NRPS; 2.
DR   FunFam; 3.30.559.10:FF:000023; Non-ribosomal peptide synthetase; 2.
DR   FunFam; 3.40.50.12780:FF:000012; Non-ribosomal peptide synthetase; 1.
DR   FunFam; 3.30.559.30:FF:000006; Yersiniabactin polyketide/non-ribosomal peptide synthetase; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 3.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   PANTHER; PTHR45527:SF10; PHENYLOXAZOLINE SYNTHASE MBTB; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF00550; PP-binding; 3.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 3.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat.
FT   CHAIN           1..2035
FT                   /note="High-molecular-weight protein 2"
FT                   /id="PRO_0000193096"
FT   DOMAIN          15..91
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REPEAT          114..146
FT                   /note="I-DR1"
FT   REPEAT          310..321
FT                   /note="I-DR2"
FT   REPEAT          378..390
FT                   /note="I-DR3"
FT   REPEAT          454..462
FT                   /note="I-DR4"
FT   REPEAT          477..491
FT                   /note="I-DR5"
FT   DOMAIN          1404..1478
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REPEAT          1495..1527
FT                   /note="II-DR1"
FT   REPEAT          1682..1693
FT                   /note="II-DR2"
FT   REPEAT          1750..1762
FT                   /note="II-DR3"
FT   REPEAT          1826..1834
FT                   /note="II-DR4"
FT   REPEAT          1849..1863
FT                   /note="II-DR5"
FT   DOMAIN          1943..2017
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          3..547
FT                   /note="I"
FT   REGION          1466..1919
FT                   /note="II"
FT   MOD_RES         52
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1439
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1977
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2035 AA;  228827 MW;  1C801377A4375BDC CRC64;
     MISGAPSKDS LLPDNRHAAD YQQLRERLIQ ELNLTPQQLH DESNLIQAGL DSIRLMRWLH
     WFRKNGYRLT LRELYAAPTL AAWNQLMLSR SPENAEEETL PDESSWPNMT ESTPFPLTPV
     QHAYLTGRMP GQTLGGVGCH LYQEFEGHCL TASQLEQAIT TLLQRHPMLH IAFRPDGQQV
     WLPQPYWNGV TVHDLRHNDA ESRQAYLDAL RQRLSHRLLR VEIGETFDFQ LTLLPDNRHR
     LHVNIDLLIM DASSFTLFFD ELNALLAGES LSAIDTRYDF RSYLLHQQKI NQPLRDDARA
     YWLAKASTLP PAPVLPLVCE PATLREVRNT RRRMIVPATR WHAFSNRAGE YGVTPTMALA
     TCFSAVLARW GGLTRLLLNI TLFDRQPLHP AVGAMLADFT NILLLDTACD GDTVSNLARK
     NQLTFTEDWE HRHWSGVELL RELKRQQRYP HGAPVVFTSN LGRSLYSSRA ESPLGEPEWG
     ISQTPQVWID HLAFEHHGEV WLQWDSNDAL FPPALVETLF DAYCQLINQL CDDESAWQKP
     FADMMPASQR AIRERVNATG APIPEGLLHE GIFRIALQQP QALAVTDMRY QWNYHELTDY
     ARRCAGRLVE CGVQPGDNVA ITMSKGAGQL VAVLAVLLAG AVYVPVSLDQ PAARREKIYA
     DASVRLVLIC QHDASAGSDD IPVLAWQQAI EAEPIVNPVV RAPTQPAYII YTSGSTGTPK
     GVVISHRGAL NTCCDINTRY QVGPHDRVLA LSALHFDLSV YDIFGVLRAG GALVMVMENQ
     RRDPHAWCEL IQRHQVTLWN SVPALFDMLL TWCEGFADAT PENLRAVMLS GDWIGLDLPA
     RYRAFRPQGQ FIAMGGATEA SIWSNACEIH DVPAHWRSIP YGFPLTNQRY RVVDERGRDC
     PDWVSGELWI GGIGVAEGYF NDSLRSEQQF LTLPDERWYR TGDLGCYWPD GTIEFLGRRD
     KQVKVGGYRI ELGEIESALS QLAGVKQATV LAIGEKEKTL AAYVVPQSEA FCVTDHRNPA
     LPKAWHTLAG TLPCCAISPE ISAEQVADFL QHRLLKLKPG HTAGADPIPL MNSLAIQPRW
     QAVVERWLAF LVTQRRLKPA AEGYQVCAGE EREDEHPHFS GHDLTLSQIL RGARNELSLL
     NDAQWSPESL AFNHPASAPY IQELATICQQ LAQRLQRPVR LLEVGTRTGR AAESLLAQLN
     AGQIEYVGLE QSQEMLLSAR QRLASWPGAR LSPWNADTLA AHAHSGDIIW LNNALHRLLP
     EDPGLLATLQ QLAVPGALLY VMEFRQLTPS ALLSTLLLTN GQPEALLHNS ADWAALFSAA
     AFNCQHSDEV AGLQRFLVQC PDRQVRRDPR QLQAALAGRL PGWMVPQRIV FLDALPLTAN
     GKIDYQALKR RHTPKAENQA EADLPQGDIE KQVAALWQQL LSTGNVTRET DFFQQGGDSL
     LATRLTGQLH QAGYEAQLSD LFNHPRLADF AATLRKIDVP VEQPFVHSPE ERYQPFALTD
     VQQAYLVGRQ PGFTLGGVGS HFFVEFEIAD LDLTRLETVW NRLIARHDML RAVVLDGQQQ
     VLEQTPPWVI PTHTLHTPEE ALRVREKLAH QVLNPEVWPV FDLQVGYVDG MPARLWLCLD
     NLLLDGLSMQ ILLAELEHGY RYPQQLLPPL PVTFRDYLQQ PSLQSPNPDS LAWWQAQLDD
     IPPAPALPLR CLPQEVETPR FARLNGALDS TRWHRLKKRA ADAHLTPSAV LLSVWSTVLS
     AWSAQPEFTL NLTLFDRRPL HPQINQILGD FTSLMLLSWH PGESWLHSAQ SLQQRLSQNL
     NHRDVSAIRV MRQLAQRQNV PAVPMPVVFT SALGFEQDNF LARRNLLKPV WGISQTPQVW
     LDHQVYESEG ELRFNWDFVA ALFPAGQVER QFEQYCALLN RMAEDESSWQ LPLAALVPPV
     KHAGQCAERP PRVCPEHSQP HIAADESTVS LICDAFREVV GESVTPAENF FEAGATSLNL
     VQLHVLLQRH EFSTLTLLDL FTHPSPVALA DYLAGVATVE KTKRPRPVRR RQRRI
//
DBGET integrated database retrieval system