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Database: UniProt
Entry: D8MSH5_ERWBE
LinkDB: D8MSH5_ERWBE
Original site: D8MSH5_ERWBE 
ID   D8MSH5_ERWBE            Unreviewed;       555 AA.
AC   D8MSH5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:CAX59782.1};
GN   Name=cheD {ECO:0000313|EMBL:CAX59782.1};
GN   OrderedLocusNames=EbC_22510 {ECO:0000313|EMBL:CAX59782.1};
OS   Erwinia billingiae (strain Eb661).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN   [1] {ECO:0000313|EMBL:CAX59782.1, ECO:0000313|Proteomes:UP000008793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eb661 {ECO:0000313|EMBL:CAX59782.1,
RC   ECO:0000313|Proteomes:UP000008793};
RX   PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA   Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA   Knaust F., Geider K., Reinhardt R.;
RT   "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT   tasmaniensis with the pear pathogen E. pyrifoliae.";
RL   BMC Genomics 11:393-393(2010).
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; FP236843; CAX59782.1; -; Genomic_DNA.
DR   RefSeq; WP_013202269.1; NC_014306.1.
DR   AlphaFoldDB; D8MSH5; -.
DR   STRING; 634500.EbC_22510; -.
DR   KEGG; ebi:EbC_22510; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_16_6; -.
DR   Proteomes; UP000008793; 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; 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; 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; PF00015; MCPsignal; 1.
DR   Pfam; PF02203; TarH; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 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|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        187..210
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"
SQ   SEQUENCE   555 AA;  59171 MW;  EE794A527668898C CRC64;
     MSVFNRIKTS SFLLCSIVAF GALQLIAGAL FLSSLSDNKD SFETASSAND KVMALTNAWY
     ALNAARADSN RVLIWLQKDG PSSSKIEGMV QHGKEQIALA DRWFKEYQSG PAIPGLDPAL
     NDRLAATYQV YSTQLSTLIG IAANRDMPGL FGLNIANDQL AMEADYNHWR DAISKLSKQA
     STRSNQAFAT MLWLLGSILL IVVFFIGLCW RVMSRVLIQP LNLALGHIRA IEQGDLTQPI
     EIDRSARNEM ARLLAGLHGM QLALVKTVGN VRASSDSILT GVSEIAAGNN DLSSRTEQQA
     ASLEQTAASM EQITATVKQN ADNSHQAAKL ALSAAETAEK GGEIVDGVIK TIFGLEESSK
     KIAEITGVIE SIAFQTNILA LNAAVEAARA GENGRGFAVV AGEVRNLAQR SAVAAKDINT
     LIAESSARVQ NGSKLAGQAE DSMQAIVVSV KQVRDIMDEI SSASDEQSKG ISQVGLAVSE
     LDRVTQQNAA LVEEASSAAQ SLEAQAAHLN SAVAVFRLTQ EAERKAVSVK SAPLRAVRKP
     AMAVASNTSE NWEAF
//
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