ID   VATB_CHLTR              Reviewed;         438 AA.
AC   O84309;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=V-type ATP synthase beta chain;
DE   AltName: Full=V-ATPase subunit B;
GN   Name=atpB; OrderedLocusNames=CT_307;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(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; AE001273; AAC67900.1; -; Genomic_DNA.
DR   PIR; A71531; A71531.
DR   RefSeq; NP_219812.1; NC_000117.1.
DR   RefSeq; WP_009871654.1; NC_000117.1.
DR   AlphaFoldDB; O84309; -.
DR   SMR; O84309; -.
DR   STRING; 813.O172_01645; -.
DR   EnsemblBacteria; AAC67900; AAC67900; CT_307.
DR   GeneID; 884817; -.
DR   KEGG; ctr:CT_307; -.
DR   PATRIC; fig|272561.5.peg.328; -.
DR   HOGENOM; CLU_022916_2_0_0; -.
DR   InParanoid; O84309; -.
DR   OMA; GFKIKPR; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
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; Reference proteome;
KW   Transport.
FT   CHAIN           1..438
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000144676"
SQ   SEQUENCE   438 AA;  48684 MW;  E295F565474A05B1 CRC64;
     MQTIYTKITD IKGNLITVEA EGASLGELVQ IERADGRSSY ASVLRFDARK VTLQVFGGTS
     GLSTGDKVIF LGRPMEVIYG DSLLGRRFNG TGKPIDREDE CFGEPIPITT PSFNPVCRIV
     PREMVRTNIP MIDMFNCLVK SQKIPIFSSS GENHNALLMR IAAQTDADIV IIGGMGLTFV
     DYNFFVKESQ RLGFADKCVM FIHKAVDAPV ECVLIPDMAL ACAERFALEQ KKNVLVLLTD
     MTAFADALKE MAITMDQIPA NRGYPGSLYS DLAVRYEKAV DIAQGGSITL ISVTTMPGDD
     ITHPVPDNTG FITEGQFYLK DNRIDPFGSL SRLKQLVIGK KTREDHGDLA NALIRLYADS
     RKSAERMSMG FKLSNWDKKL LAFSELFEAR LMSLEVNIPL EEALDIGWKI LSQSFHSEEV
     GIKEQLIQKY WPKACLHK