MCPD_KLEAK
ID MCPD_KLEAK Reviewed; 536 AA.
AC P21823; G0DZQ7;
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 aspartate transducer;
GN Name=tas; OrderedLocusNames=EAE_15540;
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: This protein responds to changes in Asp concentration in the
CC environment, transduces a signal from the outside to the inside of the
CC cell, and facilitates sensory adaptation through various levels of
CC methylation.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M26411; AAA24798.1; -; Genomic_DNA.
DR EMBL; CP002824; AEG98019.1; -; Genomic_DNA.
DR PIR; D32302; D32302.
DR RefSeq; WP_015704930.1; NC_015663.1.
DR RefSeq; YP_004593298.1; NC_015663.1.
DR AlphaFoldDB; P21823; -.
DR SMR; P21823; -.
DR STRING; 1028307.EAE_15540; -.
DR EnsemblBacteria; AEG98019; AEG98019; EAE_15540.
DR KEGG; eae:EAE_15540; -.
DR PATRIC; fig|1028307.3.peg.3108; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_16_6; -.
DR OMA; QATWLEN; -.
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..536
FT /note="Methyl-accepting chemotaxis aspartate transducer"
FT /id="PRO_0000110542"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..188
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 212..264
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 269..498
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 293
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250"
FT MOD_RES 300
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT MOD_RES 307
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250"
FT MOD_RES 489
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT MOD_RES 498
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT CONFLICT 32..50
FT /note="ALRADNHNLERITVSSQQR -> RYAPTTTILNVLPSVAST (in Ref.
FT 1; AAA24798)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..84
FT /note="AALKVPQEQVD -> GAEGAAGAGGS (in Ref. 1; AAA24798)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..130
FT /note="GGARSSLQKADLYFNQFLDTPRADEQEQQLADATRDSYENLRG -> AAPAA
FT RCKKPISILTSSSTRLARMSRNSSWPMPRVIATRIY (in Ref. 1; AAA24798)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..188
FT /note="GWS -> ALVP (in Ref. 1; AAA24798)"
FT /evidence="ECO:0000305"
FT CONFLICT 295..296
FT /note="AA -> DR (in Ref. 1; AAA24798)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..338
FT /note="GGE -> RT (in Ref. 1; AAA24798)"
FT /evidence="ECO:0000305"
FT CONFLICT 473..477
FT /note="VTQMD -> LPRY (in Ref. 1; AAA24798)"
FT /evidence="ECO:0000305"
FT CONFLICT 517..536
FT /note="Missing (in Ref. 1; AAA24798)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 58031 MW; 85AE63CA12861620 CRC64;
MFNRIRISTS LFLLLISFCI MQLISTGLSY VALRADNHNL ERITVSSQQR DALSLSWVSL
LQARNTLNRA GTRAALKVPQ EQVDALMGGA RSSLQKADLY FNQFLDTPRA DEQEQQLADA
TRDSYENLRG ALRELIVFLE NRNLQAFMDQ PTQKIQDRFE ADFVQYLQLA KATTDEASAS
SQQAYGWSIW LVAGAVLMLL VVTLSAMWWL RTMLVQPLNI IRGHFERIAS GDLSAPIEVY
GRNEISQLFA SLQRMQQSLI GTVGAVRDGA ESILIGLQEI AEGNNDLSSR TEQQAASLEE
TAASMEQLTA TVKQNADNAR QASQLARDAS STAAKGGELA DDVVTTMHDI ANSSQKIGAI
TSVIDGIAFQ TNILALNAAV EAARAGEQGR GFAVVAGEVR NLASRSAQAA KEIKLLIDES
VSRVKHGSVL VENSGATMQD IVRSVTRVTD IMGEIASASD EQSRGIEQVT QAVTQMDQVT
QQNAALVVES ASAAAALEEQ AITLADAVAV FRLADDNFVA PETSSTVKET LDCQTA
