VATB_CHLMU
ID VATB_CHLMU Reviewed; 438 AA.
AC Q9PK86;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=V-type ATP synthase beta chain;
DE AltName: Full=V-ATPase subunit B;
GN Name=atpB; OrderedLocusNames=TC_0581;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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: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; AE002160; AAF39415.1; -; Genomic_DNA.
DR PIR; D81687; D81687.
DR RefSeq; WP_010230897.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PK86; -.
DR SMR; Q9PK86; -.
DR STRING; 243161.TC_0581; -.
DR EnsemblBacteria; AAF39415; AAF39415; TC_0581.
DR GeneID; 1245940; -.
DR KEGG; cmu:TC_0581; -.
DR eggNOG; COG1156; Bacteria.
DR HOGENOM; CLU_022916_2_0_0; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 875807at2; -.
DR Proteomes; UP000000800; 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_0000144674"
SQ SEQUENCE 438 AA; 48594 MW; 36A97F0818D8AA02 CRC64;
MQTIYTRITD IKGNLITVEA EGASLGELVQ IERADGRSSY ASVLRFDAKK VTLQVFGGTS
GLSTGDKVVF LGRPMEVVYG DSLLGRRFNG TGKPIDNEEI CFGEPIPITT PSFNPVCRIV
PREMVRTNIP MIDMFNCLVK SQKIPIFSSS GENHNALLMR IAAQTDADIV IIGGMGLTFV
DYSFFVEESQ RLGFADKCVM FIHKAVDAPV ECVLIPDMAL ACAERFALEQ KKNVLVLLTD
MTAFADALKE IAITMDQIPA NRGYPGSLYS DLAVRYEKAV DIAQGGSITL ISVTTMPGDD
ITHPVPDNTG FITEGQFYLK DNRIDPFGSL SRLKQLVIGK RTREDHGDLA NALIRLYADS
RKSAERMSMG FKLSNWDKKL LAFAELFETR LMSLEVNIPL EEALDIGWKI LAQSFHSEEV
GIKEQLIQKY WPKACLHK