ID Q8F3H7_LEPIN Unreviewed; 976 AA.
AC Q8F3H7;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAN49625.1};
GN OrderedLocusNames=LA_2426 {ECO:0000313|EMBL:AAN49625.1};
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:AAN49625.1, ECO:0000313|Proteomes:UP000001408};
RN [1] {ECO:0000313|EMBL:AAN49625.1, ECO:0000313|Proteomes:UP000001408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601 {ECO:0000313|EMBL:AAN49625.1,
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 -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; AE010300; AAN49625.1; -; Genomic_DNA.
DR RefSeq; NP_712607.1; NC_004342.2.
DR RefSeq; WP_000488898.1; NC_004342.2.
DR AlphaFoldDB; Q8F3H7; -.
DR SMR; Q8F3H7; -.
DR STRING; 189518.LA_2426; -.
DR PaxDb; 189518-LA_2426; -.
DR EnsemblBacteria; AAN49625; AAN49625; LA_2426.
DR KEGG; lil:LA_2426; -.
DR PATRIC; fig|189518.3.peg.2406; -.
DR HOGENOM; CLU_012665_0_0_12; -.
DR InParanoid; Q8F3H7; -.
DR OrthoDB; 334703at2; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF13188; PAS_8; 2.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001408};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 641..693
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 698..913
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 713..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 72..99
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 884..922
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 976 AA; 108395 MW; 5EE407170124E8ED CRC64;
MFRKNLGIWI GLAITINGFV FLSIQNFRGP NPSTETNFEE QLQSVQHSSE SFLKTEESIS
EFLLYLSLGK EKETLVSSLE EIEKNLKNLR SSFSESDRKK NPAILKFDKK IGTLFSSIEE
LKEKIYRSKD IKKDTSLFLK SDFFTDLSSF RRTRLEAVKE LSNSVETASV TVVSSTPTEI
QFLVTILEYS GISILLISFL WWSNRSNQKT ILNLEMEFLR MRTAVDNVTT NIMMADRNFN
IVYMNKAIQM MFNKAESDIK KQLSNFNLSN LMGTNIDSFH KNPAHQRGLL DKLSDTFRSS
ITIGGREFDL IANPIVDVNG NKLGTVVEWS DVTEQNKIQK QRKLENEELT RVKVALDNVT
TNIMMADRNL NVVYMNKSIR AMFHSAEDDI KKQFNNFDPS RLIGTNIDIF HKNPAYQRGL
LDKLTDTFRS SINIGGRTFN LIANPIIDET GDRLGSVVEW SDVTEQNKIA EQRKIENEEL
IRVKVALDNT STNIMIADNE FNIRYMNQAV VKMFEIGEGD IKKQFAHFNL KSLVGSNIDQ
FHKNPAHQRG VLSSFTGIHK ATIKIGGRTF DLIANPILDS NGKRLGSVVE WSDVTNELAV
QEEVEGIVSA AAKGNFTTRI SLDSKTGFFL NLSRSLNQLL EVSNRGLNEV VEALERISSG
DLTQKITNEY HGTFGKLKEY SNITMDKLSE IIGDIIVRSS SLVTSASEVS STANSLSQGA
SEQAASVEET TSSLEEMTAS IDQNAQNSRQ TEQISSKSSQ DAEEGGASVI ETVKAMKQIA
EKISIIEDIA YQTNLLALNA AIEAARAGDH GKGFAVVASE VRKLAERSQK SANEISSLAG
NSVAIAEKAG NLISQIVPSI RKTADLVQEI TAASDEQSSG VSEINKAMGQ LDQVSQQNAS
ASEELAAISE EMNAQAEQLK ESVLFFKISD GDKRLTNGGG LLHRDFSGTG IIKATPTTRK
DLPKGISPIT EKFERY
//
