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Database: UniProt
Entry: M3HCB1_LEPIR
LinkDB: M3HCB1_LEPIR
Original site: M3HCB1_LEPIR 
ID   M3HCB1_LEPIR            Unreviewed;       976 AA.
AC   M3HCB1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Methyl-accepting chemotaxis protein signaling domain protein {ECO:0000313|EMBL:EMG10330.1};
GN   ORFNames=LEP1GSC151_2925 {ECO:0000313|EMBL:EMG10330.1};
OS   Leptospira interrogans serovar Grippotyphosa str. LT2186.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1001599 {ECO:0000313|EMBL:EMG10330.1, ECO:0000313|Proteomes:UP000011776};
RN   [1] {ECO:0000313|EMBL:EMG10330.1, ECO:0000313|Proteomes:UP000011776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2186 {ECO:0000313|EMBL:EMG10330.1,
RC   ECO:0000313|Proteomes:UP000011776};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., Burns M.-A.,
RA   Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., Vinetz J.M., Sutton G.G.,
RA   Nierman W.C., Fouts D.E.;
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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:EMG10330.1}.
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DR   EMBL; AFME02000259; EMG10330.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3HCB1; -.
DR   BioCyc; LINT1001599:G11K9-310-MONOMER; -.
DR   Proteomes; UP000011776; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
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   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;  108425 MW;  6A07ED2FE152660B CRC64;
     MFRKNLGIWI GLAITINGFV FLSIQNFRGP NPSTETNFEE QLQSVQHSSE SFLKTEESIS
     EFLLYLSLGK EKETLVSSLE EIEKNLKNLR SSFSESDRKK NPAILKFDKK IGTLFSSIEE
     LKEKIYRSKD LKKDTSLFLK SDFFTDLSSF RRTRLEAVKE LSNSVETASV TVVSSTPTEI
     QFLVTILEYS GISILLISFL WWSNRSNQRT 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 VKMFETGEGD IKKQFAHFNL KSLVGSNIDQ
     FHKNPAHQRG VLSSFTGIHK ATIKIGGRTF DLIANPILDT 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
//
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