ID   VATB_CHLCV              Reviewed;         438 AA.
AC   Q822J9;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=V-type ATP synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00310};
DE   AltName: Full=V-ATPase subunit B {ECO:0000255|HAMAP-Rule:MF_00310};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_00310}; OrderedLocusNames=CCA_00683;
OS   Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS   (Chlamydophila caviae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=227941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA   Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA   Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA   Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(2003).
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.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00310}.
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DR   EMBL; AE015925; AAP05425.1; -; Genomic_DNA.
DR   RefSeq; WP_011006640.1; NC_003361.3.
DR   AlphaFoldDB; Q822J9; -.
DR   SMR; Q822J9; -.
DR   STRING; 227941.CCA_00683; -.
DR   PRIDE; Q822J9; -.
DR   EnsemblBacteria; AAP05425; AAP05425; CCA_00683.
DR   KEGG; cca:CCA_00683; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_2_0_0; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000002193; 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   HAMAP; MF_00310; ATP_synth_B_arch; 1.
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; PTHR43389; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN           1..438
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000144673"
SQ   SEQUENCE   438 AA;  48292 MW;  472A35904D2F2455 CRC64;
     MQTIYTKITD IKGNLITVEA EGARLGELAE IERVDGRSSY ASVLRFDAKK VTLQVFGGTS
     GLSTGDRVIF LGRSMEVTYG ESLIGRRLNG VGKPIDGEGE CFGDPIAIST PTFNPVCRVV
     PRDMVKTNIP MIDVFNCLVK SQKIPIFSSS GESHNALLMR IAAQTDADIV IIGGMGLTFV
     DYSFFVDESK RLGFADKCVM FIHKAVDAPV ECVLIPDMAL ACAEKFAVDH NKNVLVLLTD
     MTAFADALKE IAITMDQIPA NRGYPGSLYS DLALRYEKAV DIAEGGSITL ISVTTMPGDD
     ITHPVPDNTG FITEGQFYLK NNRIDPFGSL SRLKQLVIGK VTREDHGDLA NSLIRLYADS
     RKAAERMSMG FKLSNWDKKL LAFAELFETR LMSLEVNIPL EEALDIGWKI LAQSFHSEEV
     GIKEQLINKY WPKSCLHR