ID I3I8S8_9GAMM Unreviewed; 733 AA.
AC I3I8S8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=O59_002793 {ECO:0000313|EMBL:EIK44463.1};
OS Cellvibrio sp. BR.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK44463.1, ECO:0000313|Proteomes:UP000003395};
RN [1] {ECO:0000313|EMBL:EIK44463.1, ECO:0000313|Proteomes:UP000003395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR {ECO:0000313|EMBL:EIK44463.1,
RC ECO:0000313|Proteomes:UP000003395};
RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:EIK44463.1}.
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DR EMBL; AICM01000006; EIK44463.1; -; Genomic_DNA.
DR RefSeq; WP_007643342.1; NZ_JH668202.1.
DR AlphaFoldDB; I3I8S8; -.
DR STRING; 1134474.O59_002793; -.
DR PATRIC; fig|1134474.3.peg.2626; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_6; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000003395; 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; 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:SF10; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EIK44463.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:EIK44463.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 378..585
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 587..717
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT COILED 416..443
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 733 AA; 80561 MW; E14996429D943FD0 CRC64;
MNLDAALQTF FAEAEDLLNS MEAALLRLDE GDTDPETINE IFRAAHTIKG SAGLFGLNDI
VAFTHIVENV LDRARDNKIL VTGDLLSILL PCRDHIAVLI EHAMHDHSND EECLAKGQAL
LSSLQPWLED ETAVKGVALA DPTPAMQADY IKSLVSESER ECWHISVRFG PDLLRNGMDP
LSIMRFLASL GDITHITTIT DHLPDYEHYD PEQLYLGFEI ALMSSASQQQ IEDAFMFVRD
DSELTIIPPR SNIDAYVNLI KSLPEDSKRL GEILVKSHAI SYQELDAALT MQKQQAKSQS
AVSMLGDILI EGEAVAPEIV SAALDKQKKN SERKTNPENR FIRVDAERLD TLINLIGELV
INRQRIDLLA SKMGNPTLVE AVTSMGNFTE AIRDAALTLR MVPVGDTFQK FKRVVRDTAK
SLNKEIELEI EGAETELDRS MVEKLNDPLM HIVRNAMDHG IESIAVREAR GKPAQGTIKL
TACHDAGHIV IGIHDDGGGL DVEKIRKKAI ANGILDESVH LSRQELFQLI FHPGLSTAEQ
VTNLSGRGVG MDVVKRNIEE LQGGVEIESE MGVGTSLNIR LPLTLAIIDG FHVVAGTIDF
IVPQNAILEC VDLNSLNHSH GQNCVNLRGE QVPYIRLREI FSLQGSGAER EKIVVVQFGE
KRAGIVVDEL HGEIQTVVKP MGPIFQALKG IGGSSLLGTG AVALILDIQQ LISYAINREH
LRTSALPLTA QEQ
//
