ID A0A0F4PSK2_9GAMM Unreviewed; 765 AA.
AC A0A0F4PSK2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=TW72_15735 {ECO:0000313|EMBL:KJY97256.1};
OS Pseudoalteromonas ruthenica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=151081 {ECO:0000313|EMBL:KJY97256.1, ECO:0000313|Proteomes:UP000033664};
RN [1] {ECO:0000313|EMBL:KJY97256.1, ECO:0000313|Proteomes:UP000033664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3137 {ECO:0000313|EMBL:KJY97256.1,
RC ECO:0000313|Proteomes:UP000033664};
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 -!- 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:KJY97256.1}.
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DR EMBL; JXXZ01000013; KJY97256.1; -; Genomic_DNA.
DR RefSeq; WP_045978606.1; NZ_PNCF01000016.1.
DR AlphaFoldDB; A0A0F4PSK2; -.
DR GeneID; 58229951; -.
DR PATRIC; fig|151081.8.peg.828; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000033664; 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:UP000033664};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 399..623
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 625..760
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 127..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 765 AA; 80986 MW; D512B15D489E0312 CRC64;
MSFEVDEDIL QDFLVEAGEI LEQLSEQLVE LENNPDDKDL LNAIFRGFHT VKGGAGFLGM
NELVDACHGA ENVFDILRQG KRQVTSELMD VILQALDTIN DMFALIQARE QPQPADPELL
AVLHKLSEPE SEDEAPIAVP EPAATPSEPV VEPEPVPENV ASGADDFGDD ILFDAPSADS
DEGEAIDEIT EDEFESLLDE LHGQGKGPSV GEGSADAGAS GNDEDITDDE FDSLLDELHG
AGSFGAISDN GSTPSVEEQG AAQQSAPTAS GQSESASGDD EDITEDEFDA LLDELHGKGN
APKASSAEAS PAPVEKPAAP VSQSKAKDTP PATPAPSKAP AAAKPAPSAA KGSTPPSSGD
AKKPAPKAAP PPQAETTVRV DTKRLDQIMN MVGELVLVRN RLITLANNNN SEAMGKAISN
LDVVTADLQG AVMATRMQPI KKVFGRFPRV VRDLARSLQK DISLVLEGEE TDLDKNLVEA
LADPLVHLVR NSVDHGIEMP DVREAAGKPR TGTVRLSASQ EGDHILLSIH DDGAGMDAEK
LKKIAISKGV IDHDQAARLS DTEAYNLIFA PGFSTKEEIS DISGRGVGMD VVKTKISQLN
GTINIDSQLG VGTRLDIKVP LTLAILPTLM VIVGEQTFAL PLAAVSEIFH LDLTKTNIVD
GQLTIIVREK AVPLFYLEHW LVKGADRTQR KAEGHVVIVQ IGTKKVGFVV DSLIGQEEVV
IKPLDALLQG TPGMAGATIT SDGGIALILD VPSMLKHYAG RSSVN
//
