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
//