ID ATPFD_MYCBT Reviewed; 446 AA.
AC C1AMV1;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=JTY_1342;
OS Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=561275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL Vaccine 27:1710-1716(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP010918; BAH25630.1; -; Genomic_DNA.
DR RefSeq; WP_003406697.1; NZ_CP014566.1.
DR AlphaFoldDB; C1AMV1; -.
DR SMR; C1AMV1; -.
DR GeneID; 45425281; -.
DR KEGG; mbt:JTY_1342; -.
DR HOGENOM; CLU_722652_0_0_11; -.
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; 1.20.5.620; F1F0 ATP synthase subunit B, membrane domain; 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; IPR005864; ATP_synth_F0_bsu_bac.
DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR NCBIfam; TIGR01144; ATP_synt_b; 1.
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 PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF81573; F1F0 ATP synthase subunit B, membrane domain; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Multifunctional enzyme; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..446
FT /note="ATP synthase subunit b-delta"
FT /id="PRO_0000382046"
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; 48806 MW; AF07F26E38B78315 CRC64;
MSTFIGQLFG FAVIVYLVWR FIVPLVGRLM SARQDTVRQQ LADAAAAADR LAEASQAHTK
ALEDAKSEAH RVVEEARTDA ERIAEQLEAQ ADVEAERIKM QGARQVDLIR AQLTRQLRLE
LGHESVRQAR ELVRNHVADQ AQQSATVDRF LDQLDAMAPA TADVDYPLLA KMRSASRRAL
TSLVDWFGTM AQDLDHQGLT TLAGELVSVA RLLDREAVVT RYLTVPAEDA TPRIRLIERL
VSGKVGAPTL EVLRTAVSKR WSANSDLIDA IEHVSRQALL ELAERAGQVD EVEDQLFRFS
RILDVQPRLA ILLGDCAVPA EGRVRLLRKV LERADSTVNP VVVALLSHTV ELLRGQAVEE
AVLFLAEVAV ARRGEIVAQV GAAAELSDAQ RTRLTEVLSR IYGHPVTVQL HIDAALLGGL
SIAVGDEVID GTLSSRLAAA EARLPD
//
