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Database: UniProt
Entry: A0A0B2WUL6_METAS
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ID   A0A0B2WUL6_METAS        Unreviewed;       157 AA.
AC   A0A0B2WUL6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=ATP synthase subunit 9, mitochondrial {ECO:0000256|ARBA:ARBA00019317};
DE   AltName: Full=Lipid-binding protein {ECO:0000256|ARBA:ARBA00030961};
GN   ORFNames=MAM_04784 {ECO:0000313|EMBL:KHN97187.1};
OS   Metarhizium album (strain ARSEF 1941).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHN97187.1, ECO:0000313|Proteomes:UP000030816};
RN   [1] {ECO:0000313|EMBL:KHN97187.1, ECO:0000313|Proteomes:UP000030816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHN97187.1,
RC   ECO:0000313|Proteomes:UP000030816};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC       {ECO:0000256|ARBA:ARBA00006704, ECO:0000256|RuleBase:RU004221}.
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:KHN97187.1}.
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DR   EMBL; AZHE01000011; KHN97187.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2WUL6; -.
DR   STRING; 1081103.A0A0B2WUL6; -.
DR   HOGENOM; CLU_116822_0_0_1; -.
DR   OrthoDB; 316029at2759; -.
DR   Proteomes; UP000030816; Unassembled WGS sequence.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   CDD; cd18182; ATP-synt_Fo_c_ATP5G3; 1.
DR   Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 1.
DR   HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR   InterPro; IPR000454; ATP_synth_F0_csu.
DR   InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR   InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   PANTHER; PTHR10031; ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10031:SF13; ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
PE   3: Inferred from homology;
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|RuleBase:RU004221};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU004221};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121,
KW   ECO:0000256|RuleBase:RU004221};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004221};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030816};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU004221};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU004221};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU004221}.
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004221"
FT   TRANSMEM        121..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004221"
FT   DOMAIN          84..145
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
SQ   SEQUENCE   157 AA;  16510 MW;  0211C435FFA29002 CRC64;
     MASRIFASRL ATQMATKAAR PAIRAPVAAA SKRTITGSSS PLQTLKRQQA TTLLQATSRN
     AFQVQRRAYS SEIAQAMVEV SKNLGMGSAA IGLTGAGIGI GLVFAALLNG VARNPALRGQ
     LFSYAILGFA FVEAIGLFDL MIALMAKFVR GHQNIAE
//
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