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Database: UniProt
Entry: S0NRU9_9ENTE
LinkDB: S0NRU9_9ENTE
Original site: S0NRU9_9ENTE 
ID   S0NRU9_9ENTE            Unreviewed;       176 AA.
AC   S0NRU9;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=ATP synthase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATPase subunit I {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=F-type ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE            Short=F-ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
GN   Name=atpF {ECO:0000256|HAMAP-Rule:MF_01398};
GN   ORFNames=OMQ_00772 {ECO:0000313|EMBL:EOT30079.1};
OS   Enterococcus saccharolyticus subsp. saccharolyticus ATCC 43076.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1139996 {ECO:0000313|EMBL:EOT30079.1, ECO:0000313|Proteomes:UP000014136};
RN   [1] {ECO:0000313|EMBL:EOT30079.1, ECO:0000313|Proteomes:UP000014136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43076 {ECO:0000313|EMBL:EOT30079.1,
RC   ECO:0000313|Proteomes:UP000014136};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus saccharolyticus ATCC_43076 (Illumina
RT   only assembly).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC       peripheral stalk, linking F(1) to F(0). {ECO:0000256|HAMAP-
CC       Rule:MF_01398}.
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.
CC       {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01398}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01398};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01398}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family.
CC       {ECO:0000256|ARBA:ARBA00005513, ECO:0000256|HAMAP-Rule:MF_01398,
CC       ECO:0000256|RuleBase:RU003848}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOT30079.1}.
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DR   EMBL; AHYT01000002; EOT30079.1; -; Genomic_DNA.
DR   RefSeq; WP_016174577.1; NZ_KE136523.1.
DR   AlphaFoldDB; S0NRU9; -.
DR   STRING; 41997.RV16_GL001259; -.
DR   PATRIC; fig|1139996.3.peg.766; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_4_2_9; -.
DR   OrthoDB; 282095at2; -.
DR   Proteomes; UP000014136; Unassembled WGS sequence.
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   CDD; cd06503; ATP-synt_Fo_b; 1.
DR   Gene3D; 6.10.250.1580; -; 1.
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   NCBIfam; TIGR01144; ATP_synt_b; 1.
DR   PANTHER; PTHR33445:SF1; ATP SYNTHASE SUBUNIT B; 1.
DR   PANTHER; PTHR33445; ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC; 1.
DR   Pfam; PF00430; ATP-synt_B; 1.
DR   SUPFAM; SSF81573; F1F0 ATP synthase subunit B, membrane domain; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01398};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01398};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01398}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   176 AA;  19456 MW;  6D240F1B71FA076E CRC64;
     MLNHLVLSSA EVHNTMISNF VVVTGSFVLL LVLLKIFAWD SIAAIMKKRE DKIANDLDSA
     EKSRIEAAKL EKERQMQLAN SQTEAAEIIK NARDSGESSR QTILKDAEVE VTQMRDKAHN
     DIANERQAAL SSVKDEIAGI SLQIAEKILN QELSLESHKA LIDQCIDGLG TTDEAR
//
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