ID B2FP58_STRMK Unreviewed; 701 AA.
AC B2FP58;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Transmembrane methyl-accepting chemotaxis protein I {ECO:0000313|EMBL:CAQ47998.1};
GN OrderedLocusNames=Smlt4645 {ECO:0000313|EMBL:CAQ47998.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ47998.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ47998.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ47998.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; AM743169; CAQ47998.1; -; Genomic_DNA.
DR RefSeq; WP_012481655.1; NC_010943.1.
DR AlphaFoldDB; B2FP58; -.
DR EnsemblBacteria; CAQ47998; CAQ47998; Smlt4645.
DR KEGG; sml:Smlt4645; -.
DR PATRIC; fig|522373.3.peg.4379; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_1_6; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008840};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:CAQ47998.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 396..442
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 447..676
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 647..685
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 701 AA; 73144 MW; B427A2822AB886A4 CRC64;
MSVASSRPPD TARLPHLQQL AHRADRRLLI GSAVLALAGL ALALRGPQVQ AAALAAVAVL
PAAWLGGAQA GRAVARNGLA LLLSLQLAVL CAIISLSPAL PMALLLGVLL GHRDRLPVWL
AGGVGTLALL APLQGGAALW PTLLQAGMLA GLTLFLGQVA LRLRQQTEAL GHGPRRLAAL
ARDIATGADL GAHADTGAYA PGSLAHALAD TARHVQAQRG REAASHAENA QIRQALDASR
TAMMIADNDH VIRYVNRSVV ALLRNQQATL RQAFPDFDAE RLVGSSIHRF HANPDRIRAI
LNGLQVAHNG KVQIGPVHFA QVVTPVFDAQ GVRLGFAVEW HDRTHELALE NAVAGIVAAA
AAGDLDQRLQ ATEGASFLDG LTGGINQLLD TLGSTVNEVR QMLSALANGD LDRRMHGEYH
GAFAAIQRDA NATAGQLARM VGRIQECAAS ISTAASEIAA GNGALSERSE RQAAHLQETA
ASMEELTATV RQNAAHAREA SALAASTQNA ASDGNTAMQR VVDTMQAIEG ASKRIGDITG
VIDGIAFQTN ILALNAAVEA ARAGEQGRGF AVVASEVRVL AQRSAAAAQE IKKLIDEAGR
QVGEGAQLVA DAGQRMQGIV GGVEDVSHLM REISAASQEQ SIGIEQINQT VVQMDQATQQ
NAALVEEATA AARELQNQAG TLTEAVSVFR QQEPLEVSRV A
//
