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Database: UniProt
Entry: Q04P51_LEPBJ
LinkDB: Q04P51_LEPBJ
Original site: Q04P51_LEPBJ 
ID   Q04P51_LEPBJ            Unreviewed;       522 AA.
AC   Q04P51;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ABJ77319.1};
GN   OrderedLocusNames=LBJ_2921 {ECO:0000313|EMBL:ABJ77319.1};
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=355277 {ECO:0000313|EMBL:ABJ77319.1, ECO:0000313|Proteomes:UP000000656};
RN   [1] {ECO:0000313|EMBL:ABJ77319.1, ECO:0000313|Proteomes:UP000000656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197 {ECO:0000313|EMBL:ABJ77319.1,
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; ABJ77319.1; -; Genomic_DNA.
DR   RefSeq; WP_011672118.1; NC_008510.1.
DR   AlphaFoldDB; Q04P51; -.
DR   KEGG; lbj:LBJ_2921; -.
DR   HOGENOM; CLU_522522_0_0_12; -.
DR   OMA; YIFTERA; -.
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   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 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        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        77..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        170..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          225..489
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   522 AA;  58602 MW;  03FC9B470A772B33 CRC64;
     MSKQSIESIR KKGETLTYYA RMGIMIMMLL SLASSFKALQ TQIRVIHTCG ALIMFIYSIL
     GFILYKKYEI KHWVHNLFVI LDSLTLSVTI FLDSMVSAEI IAPVLKNAIL YSVYYFIIAY
     SGLLGRPKFV LITGLISSIG YAIALTNAVF HGLQFSEDNV INMKPGYIKL SAEITKVVFM
     MGVSFILYRL MKLFDDLYQE ATSYFQENKQ FLNKLEDNRK IIHSSAETLE ISVTDFSEFT
     SLTSAKMESQ AASLEEVNAV IESLSKASEK NVDSIRIQNE NLIELNQKFQ VLLDVIAKIS
     DYSKGLDTNA KESKLEMEVV KKSVEKTSEF LKSISNSFQR VDEINRILGE IADKTNLLSL
     NASIEAARAG VAGRGFAVVA QEVSKLAEFT ATNTKMISKV VQESLEFIEE ANSASLDAGH
     STENQSIKIN LTVSKIEEMN GLYERGTMIV NDFVRNLERA KKLSDELFYS TEEQMTGQKE
     MMKAMLELEK EVNEITRESG KIQDGVLKIK TQSSDLKALS VV
//
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