ID A0A197S9S9_MYCLR Unreviewed; 446 AA. AC A0A197S9S9; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 03-AUG-2022, entry version 28. 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=A8144_04270 {ECO:0000313|EMBL:OAR19651.1}; OS Mycobacterium leprae 3125609. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1297123 {ECO:0000313|EMBL:OAR19651.1, ECO:0000313|Proteomes:UP000243179}; RN [1] {ECO:0000313|EMBL:OAR19651.1, ECO:0000313|Proteomes:UP000243179} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3125609 {ECO:0000313|EMBL:OAR19651.1, RC ECO:0000313|Proteomes:UP000243179}; RA Gupta H., Ghosh A., Mehta A., Chikara S.K.; RT "Draft genome of Mycobacterium Leprae strain 3125609."; RL Submitted (MAY-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:OAR19651.1}. 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; LYPH01000088; OAR19651.1; -; Genomic_DNA. DR RefSeq; WP_010908160.1; NZ_LYPH01000088.1. DR SMR; A0A197S9S9; -. DR EnsemblBacteria; OAR19651; OAR19651; A8144_04270. DR Proteomes; UP000243179; Unassembled WGS sequence. 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 {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 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 COILED 34..97 FT /evidence="ECO:0000256|SAM:Coils" 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 //