ID W7QBS9_9ALTE Unreviewed; 742 AA.
AC W7QBS9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DS2_12258 {ECO:0000313|EMBL:EWH09456.1};
OS Catenovulum agarivorans DS-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Catenovulum.
OX NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH09456.1, ECO:0000313|Proteomes:UP000019276};
RN [1] {ECO:0000313|EMBL:EWH09456.1, ECO:0000313|Proteomes:UP000019276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-2 {ECO:0000313|EMBL:EWH09456.1,
RC ECO:0000313|Proteomes:UP000019276};
RX PubMed=24604650;
RA Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL Genome Announc. 2:e00144-14(2014).
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC {ECO:0000256|ARBA:ARBA00035100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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:EWH09456.1}.
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; ARZY01000023; EWH09456.1; -; Genomic_DNA.
DR RefSeq; WP_035015104.1; NZ_ARZY01000023.1.
DR AlphaFoldDB; W7QBS9; -.
DR STRING; 1328313.DS2_12258; -.
DR PATRIC; fig|1328313.3.peg.2503; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000019276; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000019276};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 392..603
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 605..741
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 129..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 742 AA; 78320 MW; CB5C2DA27D9DB337 CRC64;
MSFDVDEDIL QDFLVEAAEI LEQLSEQLVE LENNPEDSDL LNAIFRGFHT VKGGAGFLAM
TALVDACHGA ENVFDILRKG QREVTPELMD VILQALDTIN VMFAQIQNRE EPEPATPELL
ETLHKLSEPA SADEPPIAAP SPTQAAPEPA GDDIEFFDNA LEDPQPSAPA QASSDGSAPL
DEITDDEFEK LLDQLHGTNK GPTSNDAPAP APAPASVASS GDEISDDEFE ALLDELHGKG
QFSTKESSSP APAPSPAPAA VTSSGDEISD DEFEALLDQL HGKGKGPNAE GSAPAPAPNP
APTPAAPAPS PTAAPAPAPK ATPAPAPSPA PAAKAPVAAS AVEKKKAPAP APAAETTVRV
DTKRLDQIMN MVGELVLVRN RLVSLGINVN DEDMSKAIAN LDVVTGDLQG AVMKTRMQPI
KKVFGRFPRV VRDLARSLNK EITLQLEGED TDLDKNLVEA LADPLVHLVR NSVDHGIEMP
DVRAANGKAR CGTVRLSASQ EGDHILLTIA DDGAGMDPEK LKEKAINNGI LDADAATRMS
DSEAYNLIFA PGFSTKEQIS DISGRGVGMD VVKTKITQLN GSVVIKSEKG VGTQLDIKVP
LTLAILPTLM VIVSGQTFAL PLAGVSEIIN LDLKKTNTVD GQLTMIVRKK AIPLFYLQDW
LTRNNNKRGD RSYGHVVVVQ VGTGKQVGFV VDSLIGQEEV VIKPLDALLQ GTPGMAGATI
TSDGGIALIL DVPGMLKKYA KR
//
