ID J1F677_9LACO Unreviewed; 685 AA.
AC J1F677;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:AJA34088.1};
GN ORFNames=FD00_GL001601 {ECO:0000313|EMBL:KRN11112.1};
OS Liquorilactobacillus mali KCTC 3596 = DSM 20444.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1046596 {ECO:0000313|EMBL:KRN11112.1, ECO:0000313|Proteomes:UP000050898};
RN [1] {ECO:0000313|EMBL:AJA34088.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 20444 {ECO:0000313|EMBL:AJA34088.1};
RX PubMed=25501479;
RA Cousin F.J., Lynch S.M., Harris H.M., McCann A., Lynch D.B., Neville B.A.,
RA Irisawa T., Okada S., Endo A., O'Toole P.W.;
RT "Detection and genomic characterization of motility in Lactobacillus
RT curvatus: confirmation of motility in a species outside the Lactobacillus
RT salivarius clade.";
RL Appl. Environ. Microbiol. 0:0-0(2014).
RN [2] {ECO:0000313|EMBL:KRN11112.1, ECO:0000313|Proteomes:UP000050898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20444 {ECO:0000313|EMBL:KRN11112.1,
RC ECO:0000313|Proteomes:UP000050898};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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};
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DR EMBL; KM886866; AJA34088.1; -; Genomic_DNA.
DR EMBL; AYYH01000004; KRN11112.1; -; Genomic_DNA.
DR RefSeq; WP_003686939.1; NZ_BACP01000046.1.
DR AlphaFoldDB; J1F677; -.
DR PATRIC; fig|1046596.6.peg.1686; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000050898; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding 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; IPR037052; CheA-like_P2_sf.
DR InterPro; IPR010808; CheA_P2-bd.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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: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 Pfam; PF07194; P2; 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}; Kinase {ECO:0000313|EMBL:AJA34088.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 303..549
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 551..683
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 259..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 94..121
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 259..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 685 AA; 76787 MW; EBA205693F71329B CRC64;
MDDNSVYRNL FFEESDDNLQ KLNDDVLELE SEPENIDLIN EIFRAAHTLK GMSATMGYNV
MTKLTHKMEN LFDFFKSGKL KVTSEYISLI FECLDKLSEL VEDLRNDQEL SEDQISELLK
KLINVEESVN GTATEKVQNT SDKTGKLTTI LESNEDADID VVKKAKAQGY NAFVVAIRID
RESMLKGPRA FLIIEHLEQE GDVIYTEPTA DLLENGEFNT DFKLIYLTKN TKEQVEANID
INSEIDTFIV EEFDSAKSAN SNEHKPLAES VSAKPTESTP KKPKSSDKKE KKSSTPSKHP
SAARNQSIRV DLTRLDLFLN LVSELVVYRN QLDDANKRSD AMEVKDSLEQ VSRLTSELQD
LVLKIRMQQV SVVFSRFPRM VRDLAKELDK DMELIVEGEE TELDKTVVSE LSEPLIHLLR
NSADHGIESA ENRKKFGKPE KGTIKLSAYQ EGNQVNITLE DDGMGIDPQV MKESAESKGI
DTTGMTDDEL INLIFHPGFS TAKKITNISG RGVGLDAVMA KINDLGGSLE MKTELHVGTK
FVIKLPLTLS IIQALMVRVA NESFAIPLDV VERVVVIQEK EIITSMDREV VEYQEGLIPV
IRVDKVLGLT NEENTKQFAI VVKSDKQYFA VLVNELIGQQ EIVIKKIDTI IQKLNKFQGA
TIFGNGSIAL ILDVNAICQG KLVEN
//
