ATPF1_RHOCS
ID ATPF1_RHOCS Reviewed; 253 AA.
AC B6IQS5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=ATP synthase subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=F-type ATPase subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE Short=F-ATPase subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF1 {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=RC1_0367;
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW;
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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DR EMBL; CP000613; ACI97811.1; -; Genomic_DNA.
DR RefSeq; WP_012565603.1; NC_011420.2.
DR AlphaFoldDB; B6IQS5; -.
DR SMR; B6IQS5; -.
DR STRING; 414684.RC1_0367; -.
DR EnsemblBacteria; ACI97811; ACI97811; RC1_0367.
DR KEGG; rce:RC1_0367; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_070737_0_0_5; -.
DR OMA; DWFTVIA; -.
DR OrthoDB; 1456190at2; -.
DR Proteomes; UP000001591; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR Pfam; PF00430; ATP-synt_B; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..253
FT /note="ATP synthase subunit b 1"
FT /id="PRO_0000368726"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 253 AA; 27562 MW; 5F08F7A4EF49BA7A CRC64;
MAIDGWTVAL QAVNFLILVL LLRHFLYRPV LAMIDRRKAE ATRLLDDAAL RVEAAKAERQ
KAETLRADLE AQADALLADS RARAGKELEE LRTRARREAD GILAEGRKAL AEERRAAEAD
LRGKAAGLAV EIAGRLLAAA TPGARVEPFL DRVCTRLTAL PEPERQVLAG QAADGGIRIV
TAVPLDEAGR AHCRDRAHTL LGPDIALTFA DDPELLAGVE LHFAHTVIRD SWRDLLGRIG
LELDGHDDAH RIA