ID E6TA88_MYCSR Unreviewed; 445 AA.
AC E6TA88;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=atpF {ECO:0000256|HAMAP-Rule:MF_01398};
GN Synonyms=atpH {ECO:0000256|HAMAP-Rule:MF_01416};
GN OrderedLocusNames=Mspyr1_17470 {ECO:0000313|EMBL:ADT98412.1};
OS Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS (Mycobacterium gilvum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=278137 {ECO:0000313|EMBL:ADT98412.1, ECO:0000313|Proteomes:UP000008916};
RN [1] {ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADT98412.1, ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RX PubMed=22180818;
RA Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT reclassification to Mycobacterium gilvum Spyr1.";
RL Stand. Genomic Sci. 5:144-153(2011).
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; CP002385; ADT98412.1; -; Genomic_DNA.
DR RefSeq; WP_013471181.1; NC_014814.1.
DR AlphaFoldDB; E6TA88; -.
DR KEGG; msp:Mspyr1_17470; -.
DR HOGENOM; CLU_722652_0_0_11; -.
DR Proteomes; UP000008916; 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 Gene3D; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 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; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR NCBIfam; TIGR01145; ATP_synt_delta; 1.
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 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 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 REGION 50..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 47879 MW; A438E846EB3BDFB4 CRC64;
MSTFIGQLIG FAVIVFIIMK WVAPLVKSMM QKQQEAIRAA LEESAEASKK LAEADAMHTK
AVEDAKSEGQ KVTDEARQDS ERITAQLAEQ ADTEAERIKS QGAQQVQLMR QQLIRQLRSG
LGAESVEKAE EIVRNYVSDP AAQASTVDRF LEELNAMAPS PAVLEAGATL NLRAASREAL
AELVKKFESV ADGADSDTLT TLADELSGVA KLLLSETTLN KHLAEPTDDS TAKTRLVERL
FDGKLGSNSL ELLKTATAQR WSSEGNLIDA LEHVARLALL ARAERDGQSE EVEDQLFRFG
RLLDSQSQLS RLLADTTVPT DKRVELLKKV VDSAGEVNGT VAALLTQTVE LLRGEPADAA
VSDLAELAVA RRGEAVAEVT AAADLSEEQR TRLTEILSRI YGTPVSVQLD VDPDVLGGLL
ITVGDEVIDG SISSRLAAAR TGLPD
//
