ID VATB1_TREPA Reviewed; 430 AA.
AC O83442;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-NOV-2024, entry version 133.
DE RecName: Full=V-type ATP synthase beta chain 1;
DE AltName: Full=V-ATPase subunit B 1;
GN Name=atpB1; OrderedLocusNames=TP_0427;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The V-type beta chain is a regulatory subunit (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AE000520; AAC65413.1; -; Genomic_DNA.
DR PIR; H71325; H71325.
DR RefSeq; WP_010881875.1; NC_021490.2.
DR AlphaFoldDB; O83442; -.
DR SMR; O83442; -.
DR IntAct; O83442; 2.
DR STRING; 243276.TP_0427; -.
DR TCDB; 3.A.2.3.3; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR EnsemblBacteria; AAC65413; AAC65413; TP_0427.
DR GeneID; 57878952; -.
DR KEGG; tpa:TP_0427; -.
DR KEGG; tpw:TPANIC_0427; -.
DR eggNOG; COG1156; Bacteria.
DR HOGENOM; CLU_022916_2_0_12; -.
DR OrthoDB; 9802718at2; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd01135; V_A-ATPase_B; 1.
DR Gene3D; 3.40.50.12240; -; 1.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR055190; ATP-synt_VA_C.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR PANTHER; PTHR43389; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR PANTHER; PTHR43389:SF4; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF22919; ATP-synt_VA_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW Transport.
FT CHAIN 1..430
FT /note="V-type ATP synthase beta chain 1"
FT /id="PRO_0000144683"
SQ SEQUENCE 430 AA; 47229 MW; 26DF2DFF3B0646D9 CRC64;
MYKVYEKIES INGSVITVRA KGVHYGELAR VKTAFGDSLA EVNKLEGDVV SLQVFAGGRG
ISTGSEVRFL GRGMLVSFSD YLLGRIFNGS GVPRDGGPAL KEGRVEIGGP SVNPAKRVIA
RRMIRTGIPM IDVFNTLVVS QKLPIFSSSG EPYNELLARI AMQAEVDVIV LGGMGLKHDD
YLYFKSALEE AGALSRAVLF VHTASDPTVE CLMVPDMCLA VAEQFALKGR DVLVLLTDMT
NFADAMKEIA IIQEQVPSNR GYPGDLYSQL ASRYEKAVDF DDAGSVTILA VTTMPGDDVT
HPVPDNTGYI TEGQFYLKNG RIEPFGSLSR LKQNVNGRTR ADHRALMDNM IKLYAAYRDA
LEKRSMGFAM SEWDEKLLTY GGLFEAQLMD LSVNIPLEEA FDTGWKILGR CFTPEETGIR
SDLINTYWPA
//
