CHEA_KLEAK
ID CHEA_KLEAK Reviewed; 652 AA.
AC P21813; G0DZQ4;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Chemotaxis protein CheA;
DE EC=2.7.13.3;
GN Name=cheA; OrderedLocusNames=EAE_15525;
OS Klebsiella aerogenes (strain ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235
OS / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56)
OS (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1028307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235 / KCTC 2190 / NBRC
RC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56;
RX PubMed=22493190; DOI=10.1128/jb.00028-12;
RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA Yang K.S.;
RT "Complete genome sequence of Enterobacter aerogenes KCTC 2190.";
RL J. Bacteriol. 194:2373-2374(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 426-652.
RC STRAIN=ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235 / KCTC 2190 / NBRC
RC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56;
RX PubMed=2496104; DOI=10.1128/jb.171.5.2361-2371.1989;
RA Dahl M.K., Boos W., Manson M.D.;
RT "Evolution of chemotactic-signal transducers in enteric bacteria.";
RL J. Bacteriol. 171:2361-2371(1989).
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 (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR EMBL; CP002824; AEG98016.1; -; Genomic_DNA.
DR EMBL; M26411; AAA24795.1; -; Genomic_DNA.
DR PIR; A32302; A32302.
DR RefSeq; WP_015704929.1; NC_015663.1.
DR RefSeq; YP_004593295.1; NC_015663.1.
DR AlphaFoldDB; P21813; -.
DR SMR; P21813; -.
DR STRING; 1028307.EAE_15525; -.
DR EnsemblBacteria; AEG98016; AEG98016; EAE_15525.
DR KEGG; eae:EAE_15525; -.
DR PATRIC; fig|1028307.3.peg.3105; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_6; -.
DR OMA; MMDMAKS; -.
DR Proteomes; UP000008881; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.10.287.560; -; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.30.70.400; -; 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; IPR015162; CheY-binding.
DR InterPro; IPR035891; CheY-binding_CheA.
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 Pfam; PF01584; CheW; 1.
DR Pfam; PF09078; CheY-binding; 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; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF50341; SSF50341; 1.
DR SUPFAM; SSF55052; SSF55052; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chemotaxis; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Transferase; Two-component regulatory system.
FT CHAIN 1..652
FT /note="Chemotaxis protein CheA"
FT /id="PRO_0000074713"
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT DOMAIN 255..507
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 509..644
FT /note="CheW-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT CONFLICT 440..442
FT /note="SDS -> TDT (in Ref. 2; AAA24795)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="A -> R (in Ref. 2; AAA24795)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..568
FT /note="DV -> EC (in Ref. 2; AAA24795)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="Y -> N (in Ref. 2; AAA24795)"
FT /evidence="ECO:0000305"
FT CONFLICT 603..604
FT /note="VV -> C (in Ref. 2; AAA24795)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="S -> T (in Ref. 2; AAA24795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 652 AA; 70609 MW; 74E89579B17A568E CRC64;
MSMDISAFYQ TFFDEADELL ADMEQHLLEL DPQAPDIEPL NAIFRAAHSI KGGAATFGFS
VLQETTHLLE NLLDGARREE MRLSTEIINL FLETKDIMQE QLDAYKTSQQ PDAESFDYIC
QALRQLALEA QQQDAPAAPP VVAQPAPTAV AGGMRVSLTG LKANEIPLML EELGNLGEVH
DPQQTDNSLE VTLLTTASEE DICAVLCFVL EPEQISFTTP PTTAAKPLPS AEVVPPPVAQ
PQPAVVEPPK APRAKASEST SIRVAVEKVD QLINLVGELV ITQSMLAQRS GNLDPVTHGD
LLNSMSQLER NARDLQESVM SIRMMPMEYV FSRYPRLVRD LAGKLNKQVE LTLQGSSTEL
DKSLIERIID PLTHLVRNSL DHGIEDPQTR LAAGKSEVGN LILSAEHQGG NICIEVIDDG
AGLNREKILA KAAAQGLAVS DSMSDEEVGM LIFAPGFSTA EQVTDVSGRG VGMDVVKRNI
QEMGGHVEIH SRAGKGTSIR ILLPLTLAIL DGMSVKVNEE VFILPLNAVM ESLQPQAEDL
HPMAGGERML QVRGEYLPLV ELYRVFDVAG AKTEATQGIV VILQSAGRRY ALLVDQLIGQ
HQVVVKNLES NYRKVPGISA ATILGDGSVA LIVDVSALQM LNREKLLSAA AA
