ATPF_KOCRD
ID ATPF_KOCRD Reviewed; 178 AA.
AC B2GLY6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=KRH_09800;
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX NCBI_TaxID=378753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX PubMed=18408034; DOI=10.1128/jb.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(2008).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01398};
CC Single-pass membrane protein {ECO:0000255|HAMAP-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; AP009152; BAG29327.1; -; Genomic_DNA.
DR AlphaFoldDB; B2GLY6; -.
DR SMR; B2GLY6; -.
DR STRING; 378753.KRH_09800; -.
DR EnsemblBacteria; BAG29327; BAG29327; KRH_09800.
DR KEGG; krh:KRH_09800; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_5_1_11; -.
DR OMA; FAWKPIL; -.
DR Proteomes; UP000008838; 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; IPR028987; ATP_synth_B-like_membr_sf.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR Pfam; PF00430; ATP-synt_B; 1.
DR SUPFAM; SSF81573; SSF81573; 1.
DR TIGRFAMs; TIGR01144; ATP_synt_b; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..178
FT /note="ATP synthase subunit b"
FT /id="PRO_0000368536"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 178 AA; 19482 MW; C46728D6EE4CF1AC CRC64;
MLAAEEANPL IPDVWEMLIT GIGFVILLFI AIKYIVPAFE KVFKDRADAI EGGLAKAKAA
QAEAKAARDE YNQQLESARL EAQKIREEAR SEGEKILADF KDRANMESAR ITENAHKAIE
AERAAAVVSL RDEVGTLATQ LASKIVGESL NDDDRANRVV DRFLADLDAE QGRTGAAR