ID A0A240C517_SERFI Unreviewed; 651 AA.
AC A0A240C517;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:SNW02869.1};
GN ORFNames=SAMEA4384070_03005 {ECO:0000313|EMBL:SNW02869.1};
OS Serratia ficaria.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=61651 {ECO:0000313|EMBL:SNW02869.1, ECO:0000313|Proteomes:UP000215134};
RN [1] {ECO:0000313|EMBL:SNW02869.1, ECO:0000313|Proteomes:UP000215134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12148 {ECO:0000313|EMBL:SNW02869.1,
RC ECO:0000313|Proteomes:UP000215134};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; LT906479; SNW02869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240C517; -.
DR STRING; 1411141.GCA_001590885_00274; -.
DR KEGG; sfj:SAMEA4384070_3005; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000215134; Chromosome 1.
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; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.30.70.400; CheY-binding domain of CheA; 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; 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 PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF55052; CheY-binding domain of CheA; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00110}; Reference proteome {ECO:0000313|Proteomes:UP000215134};
KW Transferase {ECO:0000313|EMBL:SNW02869.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 299..506
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 508..643
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT COILED 297..324
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 651 AA; 70156 MW; 83CDFEDD9467DEE8 CRC64;
MSMDISAFYQ TFFDEADELL ADMEQHLLEL DPLAPDIEPL NAIFRAAHSI KGGAATFGFS
VLQETTHLLE NLLDGARRQE MSLSTEIINL FLETKDIMQE QLDAYKTSQQ PDADSFEYIC
QALRQLALEA QQQAPAAQPA VPQAIAAPAA IEGGMRISLS GLKASEIPLM LEELGNLGEV
KDPRQTENSL EVTLLTSASE DDISAVLCFV LEPEQIAFAT PPQSEAPPEP AAAPIAEAAA
AKPAPAEAPK ARAKASESTS IRVAVEKVDQ LINLVGELVI TQSMLAQRSG NLDPVDHGDL
LNSMSQLERN ARDLQESVMS IRMMPMEYVF SRFPRLVRDL AGKLNKQVEL TLQGSSTELD
KSLIERIIDP LTHLVRNSLD HGIEDPATRV AAGKSEVGNL VLSAEHQGGN ICIEVTDDGA
GLNREKILAK AASQGLAVSD GMSDEEVGML IFAPGFSTAE QVTDVSGRGV GMDVVKRNIQ
EMGGHVEIHS QAGKGTAIRI LLPLTLAILD GMSVKVNDEV FILPLNAVME SLQPQAEDLH
PLAGGERVLQ VRGEYLPLVE LYRVFQVENA KTDATQGIVV ILQSAGRRYA LLVDQLIGQH
QVVVKNLESN YRKVPGISAA TILGDGSVAL IVDVSALQTL NREKRLTDAA A
//
