ID A0A197S9S9_MYCLR Unreviewed; 446 AA. AC A0A197S9S9; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 20-DEC-2017, entry version 15. 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}; RN [1] {ECO:0000313|EMBL:OAR19651.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3125609 {ECO:0000313|EMBL:OAR19651.1}; 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 CC presence of a proton or sodium gradient. F-type ATPases consist of CC two structural domains, F(1) containing the extramembraneous CC catalytic core and F(0) containing the membrane proton channel, CC linked together by a central stalk and a peripheral stalk. During CC catalysis, ATP synthesis in the catalytic domain of F(1) is CC coupled via a rotary mechanism of the central stalk subunits to CC proton translocation. {ECO:0000256|HAMAP-Rule:MF_01416, CC ECO:0000256|SAAS:SAAS00630369}. CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CC CF(1). It either transmits conformational changes from CF(0) to CC CF(1) or is implicated in proton conduction. {ECO:0000256|HAMAP- CC Rule:MF_01416}. CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic CC core - and F(0) - the membrane proton channel. F(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) CC has three main subunits: a(1), b(2) and c(10-14). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. F(1) is attached to F(0) by a central stalk formed by CC the gamma and epsilon chains, while a peripheral stalk is formed CC by the delta and b chains. {ECO:0000256|HAMAP-Rule:MF_01398}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01416}. Cell membrane {ECO:0000256|HAMAP-Rule:MF_01398}; CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01398}. CC -!- SIMILARITY: Belongs to the ATPase B chain family. CC {ECO:0000256|HAMAP-Rule:MF_01398}. CC -!- SIMILARITY: Belongs to the ATPase delta chain family. CC {ECO:0000256|HAMAP-Rule:MF_01416}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 ProteinModelPortal; A0A197S9S9; -. DR SMR; A0A197S9S9; -. 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 GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.520.20; -; 2. DR Gene3D; 1.20.5.620; -; 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; 2. 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|HAMAP-Rule:MF_01416, KW ECO:0000256|SAAS:SAAS00720870}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416}; KW CF(0) {ECO:0000256|HAMAP-Rule:MF_01398, KW ECO:0000256|SAAS:SAAS00630349}; KW CF(1) {ECO:0000256|HAMAP-Rule:MF_01416}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01416, KW ECO:0000256|SAAS:SAAS00720984}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01416, KW ECO:0000256|SAAS:SAAS00720869}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01416, KW ECO:0000256|SAAS:SAAS00720904}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01398, KW ECO:0000256|SAAS:SAAS00720873}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01398, KW ECO:0000256|SAAS:SAAS00721007}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01416, KW ECO:0000256|SAAS:SAAS00720903}. FT TRANSMEM 6 23 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01398}. FT COILED 34 54 {ECO:0000256|SAM:Coils}. FT COILED 70 97 {ECO:0000256|SAM:Coils}. FT COILED 275 295 {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 //