ID   Q04P55_LEPBJ            Unreviewed;       829 AA.
AC   Q04P55;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ABJ77315.1};
GN   OrderedLocusNames=LBJ_2915 {ECO:0000313|EMBL:ABJ77315.1};
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=355277 {ECO:0000313|EMBL:ABJ77315.1, ECO:0000313|Proteomes:UP000000656};
RN   [1] {ECO:0000313|EMBL:ABJ77315.1, ECO:0000313|Proteomes:UP000000656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197 {ECO:0000313|EMBL:ABJ77315.1,
RC   ECO:0000313|Proteomes:UP000000656};
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000350; ABJ77315.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q04P55; -.
DR   KEGG; lbj:LBJ_2915; -.
DR   HOGENOM; CLU_351196_0_0_12; -.
DR   Proteomes; UP000000656; Chromosome 1.
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   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 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   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        87..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        453..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          475..527
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          532..796
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   829 AA;  94211 MW;  4E049995F496CFA9 CRC64;
     MAGFPFYTSW SVFHRWVVIP SPFLGVLFLI MFFFKYPEPV SKKIMIPAFS IALSGVVVIC
     VWYFYESFSA KRVFYFSGHY WDFQVNFFYK VYAVAIIFYT FLFVGIGIWR MITLKGKDRI
     ITGIVLIPMA SIILIPGVFN AMSRDGAVSR ELYQTVLDIS LVTGLFVVLV GYINYTSEKT
     SILSRITGIT LATFFLILQI VSIFIFNQYE ESYDLIKKTE ARLSAAGLEV SKDLEYVFQY
     DPGTDSVTSL FPGNSQQPDE STLREFRFFK ITHNLFELPS LPNEEFKQSV EDILKNSPFG
     FDAYKAGVKE YLSSKNETRL SGKDIESFFD ALQNTLVVLR NKHFHLPPKE KNDPASLDKL
     FQSKIPGIDG YLRELKKFAL DPASEKRDKI FDTFLTQIRK QDKRTYKGER VYELNGPVPK
     HYISYFYVSG GKIYEVGFRY ESLREYLHPT GKILYMSAIC ILFLVLFGFR FFFQGALLNP
     LEDVVVGLRE ANSGNLEYRL QVKVEDEIGF IARSFNKMAK SIQMTRKRLH SSAETLEISV
     TDFSEFTSLT SAKMESQAAS LEEVNAVIES LSKASEKNVD SIRIQNENLI ELNQKFQVLL
     DVIAKISDYS KGLDTNAKES KLEMEVVKKS VEKTSEFLKS ISNSFQRVDE INRILGEIAD
     KTNLLSLNAS IEAARAGVAG RGFAVVAQEV SKLAEFTATN AKMISKVVQE SLEFIEEANS
     ASLDAGHSTE NQSIKINLTV SKIEEMNGLY ERGTMIVNDF VRNLERAKKL SDELFYSTEE
     QMTGQKEMMK AMLELEKEVN EITRESGKIQ DGVLKIKTQS SDLKALSVV
//