ID   B0SLD9_LEPBP            Unreviewed;       690 AA.
AC   B0SLD9;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Putative methyl-accepting chemotaxis protein McpB {ECO:0000313|EMBL:ABZ98525.1};
GN   OrderedLocusNames=LEPBI_I2436 {ECO:0000313|EMBL:ABZ98525.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ98525.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ98525.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000786; ABZ98525.1; -; Genomic_DNA.
DR   RefSeq; WP_012389386.1; NC_010602.1.
DR   AlphaFoldDB; B0SLD9; -.
DR   STRING; 456481.LEPBI_I2436; -.
DR   KEGG; lbi:LEPBI_I2436; -.
DR   HOGENOM; CLU_000445_107_12_12; -.
DR   OrthoDB; 343970at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS12025-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome I.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd12913; PDC1_MCP_like; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          332..384
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          389..653
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          394..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  76322 MW;  EF0E8B4C1727D8EE CRC64;
     MSIRQRVSLF IAGILFVGFT ILTSFQIYRT ITDLKSEIQE NANITSQKWS FQIQEHLNAM
     MGVIRGYRFA LFYASPPRDA MVSSLREILE RNDNIFGIWL CYEPNAYEGR DAAFVGKPGH
     DKSGRFVPYL HHTPDGKINF EPLADYDNPN GAGDFYLQVK KTNKAKVFGP YEYIAGGKKI
     QMISLVVPIY PKGKFLGAAG IDLDIGTLQE KIGDNRPFRG QGYISFISDN GTYVMYGQDK
     DKLGKKIQNP EHLKIYLEKL KLGEMFTIHH DGYTDYFTPF HIGKDPQFWA LQVSIPDSIL
     TEQVTKVVIS SITISLLILF VVLFFLNFVF KNLISTRLTQ AITFSSQIAS GNLATSPEEI
     NQDEIGSLLD SMNQMRNSLV SIIGDIKHTV EKLGNQSQQM ASTSQNLSDI SQTQASAAEE
     SSAAVEELSA SADNVGKSME EAVLKMKEID QSVLTLREEV QNINKEMEYL AKFASESREH
     AVVGETAMND STKAMEDIGE KAERISEVLD IITEISEKTN LLALNAAIEA ARAGDAGRGF
     AVVAEEIGKL ALQTGTSVKE IGDLVISTNS AVENGNRKVT EAAQVLNLLN NRVKEFETSA
     KRVLNSVLLQ ENNAKDIAQN SNLLTNLNLQ IEEAVFEQKR ATEEISKTII SISNGTQDVA
     SGSDQLTIVS AEIASQASYL STQVEKFKLK
//