ID C6WTU4_METML Unreviewed; 156 AA.
AC C6WTU4;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
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 OrderedLocusNames=Mmol_2335 {ECO:0000313|EMBL:ACT49235.1};
OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylotenera.
OX NCBI_TaxID=583345 {ECO:0000313|EMBL:ACT49235.1, ECO:0000313|Proteomes:UP000002742};
RN [1] {ECO:0000313|Proteomes:UP000002742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC {ECO:0000313|Proteomes:UP000002742};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT "Complete sequence of Methylotenera mobilis JLW8.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACT49235.1, ECO:0000313|Proteomes:UP000002742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC {ECO:0000313|Proteomes:UP000002742};
RX PubMed=21622745; DOI=10.1128/JB.00404-11;
RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT "Genomes of three methylotrophs from a single niche uncover genetic and
RT metabolic divergence of Methylophilaceae.";
RL J. Bacteriol. 193:3757-3764(2011).
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged
CC and duplicated form of b found in plants and photosynthetic bacteria.
CC {ECO:0000256|ARBA:ARBA00025614}.
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01398}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01398}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC membrane protein {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}.
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DR EMBL; CP001672; ACT49235.1; -; Genomic_DNA.
DR RefSeq; WP_015833270.1; NC_012968.1.
DR AlphaFoldDB; C6WTU4; -.
DR STRING; 583345.Mmol_2335; -.
DR GeneID; 80850324; -.
DR KEGG; mmb:Mmol_2335; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_4_5_4; -.
DR OrthoDB; 9788020at2; -.
DR Proteomes; UP000002742; Chromosome.
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; 1.20.5.620; F1F0 ATP synthase subunit B, membrane domain; 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}; Cell inner membrane {ECO:0000256|HAMAP-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:UP000002742};
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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01398"
SQ SEQUENCE 156 AA; 16774 MW; 3D200DF12984AB6D CRC64;
MNINFTLIAQ AIAFAVLIWF TVKFVWPPLL KAIETRQKEI ADGLAAAQEG RSALEVAAKK
SEVTLAEAKQ KASEIIAQAE KRGSQIVEEA KGNAKVEGDR ILAGAKAEID QEVNRAKEGL
RAQVSALAIA GAEKILRKEI DANAHSEMLS KLAAEL
//
