ATPFD_MYCLE
ID ATPFD_MYCLE Reviewed; 446 AA.
AC P53006;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 124.
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=ML1142;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; U15186; AAA63106.1; -; Genomic_DNA.
DR EMBL; AL583920; CAC31523.1; -; Genomic_DNA.
DR PIR; T09977; T09977.
DR RefSeq; NP_301836.1; NC_002677.1.
DR RefSeq; WP_010908160.1; NC_002677.1.
DR AlphaFoldDB; P53006; -.
DR SMR; P53006; -.
DR STRING; 272631.ML1142; -.
DR EnsemblBacteria; CAC31523; CAC31523; CAC31523.
DR KEGG; mle:ML1142; -.
DR PATRIC; fig|272631.5.peg.2064; -.
DR Leproma; ML1142; -.
DR eggNOG; COG0711; Bacteria.
DR eggNOG; COG0712; Bacteria.
DR HOGENOM; CLU_722652_0_0_11; -.
DR OMA; YVVPPVR; -.
DR Proteomes; UP000000806; 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: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 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; PTHR11910; 1.
DR Pfam; PF00430; ATP-synt_B; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF81573; SSF81573; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Multifunctional enzyme; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..446
FT /note="ATP synthase subunit b-delta"
FT /id="PRO_0000193472"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..168
FT /note="ATP synthase subunit b"
FT REGION 169..446
FT /note="ATP synthase subunit delta"
SQ SEQUENCE 446 AA; 48939 MW; E35E4DC96E46AD8B CRC64;
MSTFIGQLVG FAAIVYLVWW YVVPPVCRLM RARRDAVRQQ LTEAAEAADR LVEASQAHTK
ATEDAKVEAQ RVVKEAVEDA KRIVEQLQAQ ADVEAERIKL QGARQVELLR AQLTRQLRLK
FGHESVRQAA ELVRNHVADA VQQSATVDRF LDDLDAMTPK GADVEYPLLA KMRSASRRAL
VDLADRFGAI AKSLDNQALY TLAGELVSVA KMLDREIVVT RYLTVPVEDE APRVKLIDRL
VSAHVGDPTM EILRAAVSER WSANTDLVDA LEHISRQALL EVAEREDQID EVEDQVFRFS
RILDVAPRLA ILLDDYAVPA DSRVRLLCNV LQSASSVVNP IAVALLSQTV ELLRGQPAKE
AILFLAEVAV ARRGEVVAQV SAAAEISDAQ RTRLTEVLSR IYGHPVTVQM QIDAALLGGL
SIVVGDEVID GTLSSCLVAA EAALPD
