ID B4EYX3_PROMH Unreviewed; 575 AA.
AC B4EYX3;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:CAR45536.1};
GN OrderedLocusNames=PMI2809 {ECO:0000313|EMBL:CAR45536.1};
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR45536.1, ECO:0000313|Proteomes:UP000008319};
RN [1] {ECO:0000313|EMBL:CAR45536.1, ECO:0000313|Proteomes:UP000008319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR45536.1,
RC ECO:0000313|Proteomes:UP000008319};
RX PubMed=18375554; DOI=10.1128/JB.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; AM942759; CAR45536.1; -; Genomic_DNA.
DR RefSeq; WP_012368515.1; NC_010554.1.
DR AlphaFoldDB; B4EYX3; -.
DR EnsemblBacteria; CAR45536; CAR45536; PMI2809.
DR GeneID; 6800258; -.
DR KEGG; pmr:PMI2809; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_16_6; -.
DR Proteomes; UP000008319; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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 Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 191..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 215..269
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 274..503
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 537..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 64296 MW; 2AD829B393300279 CRC64;
MLKRIKISSG LMFILILFCA IQLFSGATGI RDAYLTNKRI SQLADGFEQI KTMDYGYAAL
NKLREDMLNV MFDAHLTPDL AESKITDFLS SYPQRKKEVS SIITQYFTSA ENADFDREKV
AKMKKLFQRV IYDLDQLVSC LEIRDYYGFQ SLYAHNTNER FTQSLYEATD HLSDNVVNHA
IEAAQGNYQR ALIFAFIFMS VFILFTVFVM LWIRHHIVLR IKQVIDYMSD ISQGNLLENS
TIKAKGNNEI DQLINGIQYM RSELSLIVNA IRGTSHHIYN GVQELSAGNN DLSSRTQEQA
SALEETASSM EQLTATVKNN TESAREVSHL INQTSNIASK GGDVTHRMVK TMNDIAQSSQ
KIGEITTVIN SIAFQTNILS LNAAVEAARA GEQGRGFSVV ATEVRELAQR SAEAAKEIKE
LIDASINRVK QGNQLVEQVS TSMDEILTSV KHVESSMTEI LSASEEQTRG ISQVSLAVTE
MDKATQQNAA MVEQSSAVAS LLTEEAGDLE QIVEQFKTAE SLFSKKSTLT KPVEKSANIG
LSPIKENQQD SRIKEPKNHN QSTFKEDEDD DWTSF
//
