ID A0A0F6A5I6_9GAMM Unreviewed; 313 AA.
AC A0A0F6A5I6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Chemotaxis protein CheW {ECO:0000313|EMBL:KKE81106.1};
GN ORFNames=N479_03630 {ECO:0000313|EMBL:KKE81106.1};
OS Pseudoalteromonas luteoviolacea S4054.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE81106.1, ECO:0000313|Proteomes:UP000033434};
RN [1] {ECO:0000313|EMBL:KKE81106.1, ECO:0000313|Proteomes:UP000033434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4054 {ECO:0000313|EMBL:KKE81106.1,
RC ECO:0000313|Proteomes:UP000033434};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKE81106.1}.
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DR EMBL; AUXW01000198; KKE81106.1; -; Genomic_DNA.
DR RefSeq; WP_046358412.1; NZ_AUXW01000198.1.
DR AlphaFoldDB; A0A0F6A5I6; -.
DR PATRIC; fig|1129367.4.peg.5138; -.
DR Proteomes; UP000033434; Unassembled WGS sequence.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd19924; REC_CheV-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.40.50.180; CheA-289, Domain 4; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR024181; Chemotax_regulator_CheV.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR47233; CHEMOTAXIS PROTEIN CHEV; 1.
DR PANTHER; PTHR47233:SF4; CHEMOTAXIS SIGNAL TRANSDUCTION PROTEIN-RELATED; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF002867; CheV; 1.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 19..162
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 184..309
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 242
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 313 AA; 35238 MW; 4854989CA9FDEED1 CRC64;
MAGVLASVDQ RTQLVGENRL ELLLFHLHSR HLFALNVFKV KEVVKLPHLN KMPNAHPKVA
GVTNIRGESI PVIDLRQAIC MPPTEYDDDS NLVITEYNRT VQAFLVGKVD HIVNTTWSDI
MPTPKTVGRN HYLTALTKVQ RDGVEHIVEI IDVEKVLAEI IDYDIEIPEG VLDQSILNQF
QGRKILHADD SATARRQVSD TLAQIGIEII PATDGQEALN LLKHWADEGI DVNKELMAVI
TDAEMPVMDG YRLTYEIRND DRLKDLYVIL NTSLSGSFNQ AMVEKVGCNA FLSKFQPDLL
VQEMQKRLKQ ILG
//