ID H6MW41_GORPV Unreviewed; 449 AA.
AC H6MW41;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01398, ECO:0000256|HAMAP-Rule:MF_01416};
DE Includes:
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};
DE Includes:
DE RecName: Full=ATP synthase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE AltName: Full=F-type ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE Short=F-ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
GN Name=atpFH {ECO:0000313|EMBL:AFA72855.1};
GN Synonyms=atpF {ECO:0000256|HAMAP-Rule:MF_01398}, atpH
GN {ECO:0000256|HAMAP-Rule:MF_01416};
GN OrderedLocusNames=GPOL_c18070 {ECO:0000313|EMBL:AFA72855.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA72855.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA72855.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(2012).
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 -!- FUNCTION: This fusion protein includes a component of the F(0) channel
CC (subunit b) and of the F(1) subunit (subunit delta). Two copies of
CC subunit b and one of delta together form the peripheral 'stator' stalk
CC which links F(1) to F(0). {ECO:0000256|ARBA:ARBA00024925}.
CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CF(1).
CC It either transmits conformational changes from CF(0) to CF(1) or is
CC implicated in proton conduction. {ECO:0000256|HAMAP-Rule:MF_01416}.
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|ARBA:ARBA00025830, ECO:0000256|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01416}. Cell
CC membrane {ECO:0000256|ARBA:ARBA00004162, ECO:0000256|HAMAP-
CC Rule:MF_01398}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004162, 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. {ECO:0000256|HAMAP-
CC Rule:MF_01398}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01416}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ATPase delta
CC chain family. {ECO:0000256|ARBA:ARBA00010377}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ATPase B chain
CC family. {ECO:0000256|ARBA:ARBA00010811}.
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DR EMBL; CP003119; AFA72855.1; -; Genomic_DNA.
DR RefSeq; WP_006368523.1; NC_016906.1.
DR AlphaFoldDB; H6MW41; -.
DR STRING; 1112204.GPOL_c18070; -.
DR KEGG; gpo:GPOL_c18070; -.
DR eggNOG; COG0711; Bacteria.
DR eggNOG; COG0712; Bacteria.
DR HOGENOM; CLU_722652_0_0_11; -.
DR Proteomes; UP000009154; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
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 HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1.
DR PANTHER; PTHR11910:SF1; ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL; 1.
DR Pfam; PF00430; ATP-synt_B; 1.
DR Pfam; PF00213; OSCP; 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 membrane {ECO:0000256|HAMAP-Rule:MF_01398};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01398};
KW CF(1) {ECO:0000256|HAMAP-Rule:MF_01416};
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01398"
FT COILED 34..68
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 449 AA; 48452 MW; 2B129150D649F685 CRC64;
MDIFIGQLVG FLVIVAIFVK WVLPPLRKAV LAQKDAISQQ IVESEEAKSR AEDARVAHDR
AVEKAEAEAK ELHAGALEDA KSIEEDLKAL ADAEVRRISE HGKSQAELAR TSLVRQLRLE
LGLNAVDGAG EIVRRHLSSA DNQSAAIDRA INELDGMAAG QADSSVPASS ELIGLHSLHA
TSRDAARAVG AEFESAAKDL DAQALTSASE EMASVIKFLL DNPVLRKKLT EDEDNDAGKK
QMVHTLLDGK VAPIVVDTVA SAAAQRWSQS LDFVTALRRQ NALIVLTAAE RDGTIEQTED
ELFRVGRLLD ANPEFASLLA DFQRPADGRV ELLRSLIGDQ VGPHTWYLLS HTVALLHGQP
SETAVAHLAE LAAARRGEIV AHVVSAVELT DEQRTRLAQV LGNIYHRTIS VQTEVDESII
GGLRIGVGDE VIEADIATRL AKATETLPR
//
