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Database: UniProt
Entry: A0A1X1V6S5_9MYCO
LinkDB: A0A1X1V6S5_9MYCO
Original site: A0A1X1V6S5_9MYCO 
ID   A0A1X1V6S5_9MYCO        Unreviewed;       446 AA.
AC   A0A1X1V6S5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=atpH {ECO:0000256|HAMAP-Rule:MF_01416};
GN   Synonyms=atpF {ECO:0000256|HAMAP-Rule:MF_01398};
GN   ORFNames=AWC06_06590 {ECO:0000313|EMBL:ORV64719.1};
OS   Mycobacterium fragae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1260918 {ECO:0000313|EMBL:ORV64719.1, ECO:0000313|Proteomes:UP000194000};
RN   [1] {ECO:0000313|EMBL:ORV64719.1, ECO:0000313|Proteomes:UP000194000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45731 {ECO:0000313|EMBL:ORV64719.1,
RC   ECO:0000313|Proteomes:UP000194000};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORV64719.1}.
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DR   EMBL; LQOW01000003; ORV64719.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1V6S5; -.
DR   STRING; 1260918.AWC06_06590; -.
DR   OrthoDB; 5242917at2; -.
DR   Proteomes; UP000194000; Unassembled WGS sequence.
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   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; 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   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:UP000194000};
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   COILED          34..82
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   446 AA;  48973 MW;  0169397808E27FAA CRC64;
     MSTFFGQLAG FAVIVLLVWR YVVPPVRRLM TERQETVRQE LEDSAAAAKR LEEAGQAHAQ
     ALEEAKAEAR RITEEAHADA ERIAEQLHAQ ADAEVERIKQ QGAKQVELMR AQLIRQLRQD
     IGTESVRRAG DLVRGYVADS EQQSATVDRF LDDLDAMAPS DAEVEYPVLA KMRSASRRSL
     DALVDRFGEI ADGLDDKALS TLAEELASVA ALLNREIVVT RYLTVPAEDA APRIRLIERL
     VADKVGDTTL DILRSAVSQR WSTNSDLVDA VEHIARQALL MRAERAGQVD EVEDQLFRFS
     RILDAQPRLA ILLGDYAVPP EGRVQLLRNV LDSASGRVNP IAAELLSQTV ELLRGQPAEE
     AVLGLAEVAV ARRGEVVAHV TAAAELTDRQ LERLTEVLSR IYSHPVTVQM QIDPEVLGGL
     SITVGDEVID GTLSSRLAAA ETQLPD
//
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