ATPFD_MYCVP
ID ATPFD_MYCVP Reviewed; 445 AA.
AC A1TD58;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=ATP synthase subunit b-delta;
DE Includes:
DE RecName: Full=ATP synthase subunit b;
DE AltName: Full=ATP synthase F(0) sector subunit b 2;
DE AltName: Full=ATPase subunit I 2;
DE AltName: Full=F-type ATPase subunit b 2;
DE Short=F-ATPase subunit b 2;
DE Includes:
DE RecName: Full=ATP synthase subunit delta;
DE AltName: Full=ATP synthase F(1) sector subunit delta;
DE AltName: Full=F-type ATPase subunit delta;
DE Short=F-ATPase subunit delta;
GN Name=atpFH; Synonyms=atpF, atpH; OrderedLocusNames=Mvan_4331;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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) (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ATPase B chain
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ATPase delta
CC chain family. {ECO:0000305}.
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DR EMBL; CP000511; ABM15108.1; -; Genomic_DNA.
DR RefSeq; WP_011781486.1; NC_008726.1.
DR AlphaFoldDB; A1TD58; -.
DR SMR; A1TD58; -.
DR STRING; 350058.Mvan_4331; -.
DR EnsemblBacteria; ABM15108; ABM15108; Mvan_4331.
DR KEGG; mva:Mvan_4331; -.
DR eggNOG; COG0711; Bacteria.
DR eggNOG; COG0712; Bacteria.
DR HOGENOM; CLU_722652_0_0_11; -.
DR OMA; YVVPPVR; -.
DR OrthoDB; 1937493at2; -.
DR Proteomes; UP000009159; 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 Gene3D; 1.10.520.20; -; 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 PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00430; ATP-synt_B; 1.
DR Pfam; PF00213; OSCP; 1.
DR SUPFAM; SSF47928; SSF47928; 1.
DR SUPFAM; SSF81573; SSF81573; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Multifunctional enzyme; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..445
FT /note="ATP synthase subunit b-delta"
FT /id="PRO_0000368898"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..168
FT /note="ATP synthase subunit b"
FT REGION 169..445
FT /note="ATP synthase subunit delta"
SQ SEQUENCE 445 AA; 47283 MW; FE50A8826F0E4BBD CRC64;
MSIFIGQLIG FAVIVFILVK WVVPPIKGLM QKQQEAVRVA LAESAEAGKK LADADAMHAK
AVEDAKAAGA KVTEEAQQDS QRITAQLAEQ ADAEAERIKA QGAQQVQLMR QQLIRQLRSG
LGSESVQKAE EIVRNYVSDP AAQASTVDRF LDELDAMAPS SAVLEAGASL NLRAASREAL
AELVKKFESV AESADTAALA TLADNLSAVA RLLLTSATLD KHLAEPTGDS AAKVRLLERL
FGGKVDDNTM DLLKTAVAQR WSTEGNLIDA VEHVARLALL VRAEREGQSE EVEDQLFRFG
RVLDAQSQLS RLLADPVIPA DKRVALLKKV LDSGGGVNPI AEALLTQTVE LIRGASADDA
VNDLAELAVA RRGEAVAQVT AAADLSDAQR TRLTEVLSRI YGTPVSIQLE VDPEVLGGLL
ITVGDEVIDG SISSRLAAAR TGLPD
