MCPS_KLEAK
ID MCPS_KLEAK Reviewed; 556 AA.
AC P21822; G0DZQ6;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Methyl-accepting chemotaxis serine transducer;
GN Name=tse; OrderedLocusNames=EAE_15535;
OS Klebsiella aerogenes (strain ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235
OS / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56)
OS (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1028307;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235 / KCTC 2190 / NBRC
RC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56;
RX PubMed=2496104; DOI=10.1128/jb.171.5.2361-2371.1989;
RA Dahl M.K., Boos W., Manson M.D.;
RT "Evolution of chemotactic-signal transducers in enteric bacteria.";
RL J. Bacteriol. 171:2361-2371(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235 / KCTC 2190 / NBRC
RC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56;
RX PubMed=22493190; DOI=10.1128/jb.00028-12;
RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA Yang K.S.;
RT "Complete genome sequence of Enterobacter aerogenes KCTC 2190.";
RL J. Bacteriol. 194:2373-2374(2012).
CC -!- FUNCTION: Receptor for the attractant L-serine and related amino acids.
CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the
CC concentration of attractants and repellents in the environment,
CC transduce a signal from the outside to the inside of the cell, and
CC facilitate sensory adaptation through the variation of the level of
CC methylation. Attractants increase the level of methylation while
CC repellents decrease the level of methylation, the methyl groups are
CC added by the methyltransferase CheR and removed by the methylesterase
CC CheB.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; M26411; AAA24797.1; -; Genomic_DNA.
DR EMBL; CP002824; AEG98018.1; -; Genomic_DNA.
DR PIR; C32302; C32302.
DR RefSeq; WP_015367342.1; NC_015663.1.
DR RefSeq; YP_004593297.1; NC_015663.1.
DR AlphaFoldDB; P21822; -.
DR SMR; P21822; -.
DR STRING; 1028307.EAE_15535; -.
DR EnsemblBacteria; AEG98018; AEG98018; EAE_15535.
DR KEGG; eae:EAE_15535; -.
DR PATRIC; fig|1028307.3.peg.3107; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_16_6; -.
DR OMA; HMQNELI; -.
DR Proteomes; UP000008881; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; cd00181; Tar_Tsr_LBD; 1.
DR InterPro; IPR035440; 4HB_MCP_dom_sf.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR004091; Chemotax_Me-accpt_rcpt_Me-site.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SMART; SM00319; TarH; 1.
DR SUPFAM; SSF47170; SSF47170; 1.
DR PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Chemotaxis; Membrane; Methylation;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..556
FT /note="Methyl-accepting chemotaxis serine transducer"
FT /id="PRO_0000110543"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..191
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..556
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 216..268
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 273..502
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 64..73
FT /note="The 3 Arg may form a positively charged pocket,
FT which binds the alpha-carboxyl group of the attractant AA"
FT /evidence="ECO:0000250"
FT MOD_RES 297
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250"
FT MOD_RES 304
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT MOD_RES 311
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250"
FT MOD_RES 493
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT MOD_RES 502
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT CONFLICT 35
FT /note="S -> G (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="A -> AE (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="E -> K (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
FT CONFLICT 145..146
FT /note="EG -> GGC (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
FT CONFLICT 276..279
FT /note="AIYS -> RSID (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="I -> S (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="S -> A (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="G -> V (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="G -> A (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="A -> R (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="Missing (in Ref. 1; AAA24797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 60038 MW; F2DE0FCA1865C9A5 CRC64;
MFNRIKVVTS LLLVLVLFGA LQLISGGLFF SSLKSDKENF TVLQTIRQQQ LLLSESRVDL
LQARNSLNRA GIRYMMDTNK IGSGATIDEL LAKAKEELAR AERNYTAYEK IPQDPRQDPQ
ATEKLKQQYG ILYGALSELI QLLGEGKINA FFDQPTQKYQ DDFEQTYNAY LQQNGKLYQI
AVDASNSSYS SAIWTLIVVI IVVLAAIVGV WMGIHHILVR PLNRMIEHIK RIASGDLTQP
IPVTSRNEIG VLAASLKHMQ NELIETVSGV RQGADAIYSG ASEIAAGNND LSSRTEQQAA
SLEETAASME QLTATVKQNA ENARQASQLA LSASETAQKG GKVVANVVET MHDIASSSQK
IADITGVIDG IAFQTNILAL NAAVEAARAG EQGRGFAVVA GEVRNLAQRS AQAAKEIKAL
IEDSVNRVDM GSVLVESAGD TMGDIVNAVT RVTDIMGEIA SASDEQSRGI DQVGQAVAEM
DRVTQQNASL VEESASAAAA LEEQASLLTQ SVAVFRLKSE GQEEYKAPVS NKTAPAAIAT
HKKTSASDYQ DNWETF
