ID A0A5R2BKY8_9LEPT Unreviewed; 402 AA. AC A0A5R2BKY8; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 27-MAR-2024, entry version 10. DE SubName: Full=Formate hydrogenase {ECO:0000313|EMBL:TGM85738.1}; GN ORFNames=EHR00_02170 {ECO:0000313|EMBL:TGM85738.1}; OS Leptospira levettii. OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae; OC Leptospira. OX NCBI_TaxID=2023178 {ECO:0000313|EMBL:TGM85738.1, ECO:0000313|Proteomes:UP000297645}; RN [1] {ECO:0000313|EMBL:TGM85738.1, ECO:0000313|Proteomes:UP000297645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=201601122 {ECO:0000313|EMBL:TGM85738.1, RC ECO:0000313|Proteomes:UP000297645}; RA Vincent A.T., Schiettekatte O., Bourhy P., Veyrier F.J., Picardeau M.; RT "Revisiting the worldwide diversity of Leptospira species in the RT environment."; RL PLoS Negl. Trop. Dis. 0:0-0(2019). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141, CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}. 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:TGM85738.1}. 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; RQHM01000004; TGM85738.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5R2BKY8; -. DR Proteomes; UP000297645; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001750; ND/Mrp_mem. DR PANTHER; PTHR42682; HYDROGENASE-4 COMPONENT F; 1. DR PANTHER; PTHR42682:SF5; HYDROGENASE-4 COMPONENT F; 1. DR Pfam; PF00361; Proton_antipo_M; 1. PE 4: Predicted; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6..25 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 32..51 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 57..76 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 88..109 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 129..150 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 171..188 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 194..217 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 229..247 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 253..277 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 298..318 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 333..354 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 374..398 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 53..344 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" SQ SEQUENCE 402 AA; 45560 MW; 033BD2222F6E0B82 CRC64; MMEIVFYLSG IITFVVIFLI SIFAPTKGQT RIWLWSLLKI CFFTVLFYSW FTDNIVLKWI LIEASTLFGA LLISSSGTER SFHVGWKFLL INSYALGLAF LGIVILLFAS TPLQNLDFSS LKLGLEGQSG LLIETGILLT IYGYSGKLGL VPNHFWVGDT YAESPSQISS LIASFVPVSV VLAIRPLIKL ENELNLHLIN ASNGLLFIGI LTILYSTLML VSRDDIRRIS AKVALFHTGM LTLFLWLDIS DDVFYYLLAT TVLVKLLVFL SMGILRMDAG KRNISQILNG TMLSHKALYV YLLALLIAFV FPLSPVFVLD LKIIEIAIMK KQFYLFIFPI LGSVFFFVSL NKVLPMVKLE NRDFNSEVYG TLQLRFYFFW FSLLFTISVG AYGMYYLMAK YI //