ID Q8F9P1_LEPIN Unreviewed; 606 AA. AC Q8F9P1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-NOV-2024, entry version 138. DE SubName: Full=ATPase and permease components of ABC-type multidrug transport system {ECO:0000313|EMBL:AAN47349.1}; GN Name=mdlB {ECO:0000313|EMBL:AAN47349.1}; GN OrderedLocusNames=LA_0150 {ECO:0000313|EMBL:AAN47349.1}; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain OS 56601). OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae; OC Leptospira. OX NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN47349.1, ECO:0000313|Proteomes:UP000001408}; RN [1] {ECO:0000313|EMBL:AAN47349.1, ECO:0000313|Proteomes:UP000001408} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601 {ECO:0000313|EMBL:AAN47349.1, RC ECO:0000313|Proteomes:UP000001408}; RX PubMed=12712204; DOI=10.1038/nature01597; RA Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X., RA Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., Gu W.Y., RA Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., Wan M., RA Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., Qiang B.Q., RA Xia Q.C., Guo X.K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.M., RA Shi M.H., Chen Z., Xu J.G., Zhao G.P.; RT "Unique physiological and pathogenic features of Leptospira interrogans RT revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. 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; AE010300; AAN47349.1; -; Genomic_DNA. DR RefSeq; NP_710331.1; NC_004342.2. DR RefSeq; WP_000828456.1; NC_004342.2. DR AlphaFoldDB; Q8F9P1; -. DR STRING; 189518.LA_0150; -. DR PaxDb; 189518-LA_0150; -. DR EnsemblBacteria; AAN47349; AAN47349; LA_0150. DR KEGG; lil:LA_0150; -. DR PATRIC; fig|189518.3.peg.154; -. DR HOGENOM; CLU_000604_84_3_12; -. DR InParanoid; Q8F9P1; -. DR OrthoDB; 9804259at2; -. DR Proteomes; UP000001408; Chromosome I. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR CDD; cd07346; ABC_6TM_exporters; 1. DR FunFam; 3.40.50.300:FF:000299; ABC transporter ATP-binding protein/permease; 1. DR FunFam; 1.20.1560.10:FF:000134; ABC transporter transmembrane region; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR039421; Type_1_exporter. DR PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1. DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000001408}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 63..80 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 100..120 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 174..197 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 203..222 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 294..311 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 64..346 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000259|PROSITE:PS50929" FT DOMAIN 379..606 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 19..39 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 606 AA; 68077 MW; AF79FD8E10CB5F1B CRC64; MKRPLEYNPE LIQKSEPLPE KGSSKKWKVP NPKKEKAGSE TEGAPSLLIF GLFRFAKKYK GRIFLIIGLL CFEIGFYASI PFSFKYLIDE ALINRNQNAL YWIGAYLAIG TIAFAILGTL RDYLYNWASA RIIQDLRLQM YEHLDQLSLD FFSNNKLGDI LSRFFNDLTA LEHALLAFIP WGLGPLLEAV FGTILLFLLD WKLALIALLI WPISFLGPGF LSRKSTEISY TRKLEEAQVL SLVEESISAQ NLIRAYDLSD YFFARFKNNC EKLFQVSLRL GLTNSYLERS AGSGILLLQG VLLLVGTIFA YHNTLSIGTL AAFLPPFLNL SYSLLYLSQY LPALNHASGS AKRILELLRT PVFESNPEES SIPELKEAIH FENVHFRYKG RSKNLSDITL TISKGSYTAI VGGSGVGKST FIKLLLGMVQ PNEGRILFDG MDINLLSRSS VRSLVGVVFQ ETFLFNTTIF ENIRIGKPSA TLEEVIEAAK RAEIHETILS LPMGYETNAG DRGTKLSGGE RQRIAIARAF LRNPQILLLD EATSSLDPVT EARIMKTLSL LREGRTVISV THRLSTIREA DQVFQMRNGK LERFSVPEPE QQAMVL //