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Database: UniProt
Entry: P21822
LinkDB: P21822
Original site: P21822 
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   27-MAR-2024, entry version 138.
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; Pseudomonadota; 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   KEGG; eae:EAE_15535; -.
DR   PATRIC; fig|1028307.3.peg.3107; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_16_6; -.
DR   OrthoDB; 9765776at2; -.
DR   Proteomes; UP000008881; 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   CDD; cd19407; Tar_Tsr_sensor; 1.
DR   Gene3D; 1.20.120.30; Aspartate receptor, ligand-binding domain; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 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   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; SM00304; HAMP; 1.
DR   SMART; SM00283; MA; 1.
DR   SMART; SM00319; TarH; 1.
DR   SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 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
//
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