ID A0A011MZZ6_9PROT Unreviewed; 646 AA.
AC A0A011MZZ6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA_1 {ECO:0000313|EMBL:EXI68161.1};
GN ORFNames=AW08_01379 {ECO:0000313|EMBL:EXI68161.1};
OS Candidatus Accumulibacter adjunctus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI68161.1, ECO:0000313|Proteomes:UP000020218};
RN [1] {ECO:0000313|EMBL:EXI68161.1, ECO:0000313|Proteomes:UP000020218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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:EXI68161.1}.
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DR EMBL; JFAX01000006; EXI68161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011MZZ6; -.
DR STRING; 1454001.AW08_01379; -.
DR PATRIC; fig|1454001.3.peg.1429; -.
DR Proteomes; UP000020218; 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: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:UP000020218};
KW Transferase {ECO:0000313|EMBL:EXI68161.1}.
FT DOMAIN 3..107
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 265..497
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 499..628
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 132..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 646 AA; 69480 MW; 142F7814C224A1E1 CRC64;
MSDFAGMEDL LQDFLQEAGD LLSDVDNKLV DLERSPEDLG LLNDIFRGFH TIKGGAGFLN
AGELVKLCHL TENLFDRLRN GEKELTPALM DTIMAATQGV RQMFGEIAQG RQPFPAAAEV
TANLQSALTT AADPGATSPV AAEPRAGGPA GPAVATGSGE QGPDWQALHA AVIGGQPAVS
LPAVARTAAT APAGKQADEV ELSQLQPHFP PEGRRSTDRP GAAASAAPSG RRADERAAAR
ETTIRVDTAR LDQVLNLSGE IGLTKNRLTS LRADILAGRT DSDTLQALDQ AVSQLDLLVS
DLQNSVMKTR MQPIGRLFQK YPRIARDLAR QLGKDVELAL IGEETEVDKT MIEDLADPLI
HLIRNAVDHG VESPDERRAA GKQAKSVIRL EARQEGDHIV LMIADDGRGM SPERIRAKAV
EKRIISEEDA NTLDDRQSLN LIFLPGFSTM AKASAVSGRG VGMDVVKTNI QKLNGSIEIR
SEPGKGSVFV ISLPLTLAIL PVLLVLLEEQ PFALPLSLVR EILPIDHERM QEVGGRETLV
VRGEILPVIA LAHLLGWPQV RRPEFGVLMQ TAERSFILAV DNFAGRDDAV IKALDDFRPR
GVAGVTTLSN GQIVLILDMK ELLSDLAAKG ERDTRTTAPR ALELLV
//
