ID A0A843YNA8_9BURK Unreviewed; 2000 AA.
AC A0A843YNA8;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GEV47_11695 {ECO:0000313|EMBL:MQR01339.1};
OS Glaciimonas soli.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Oxalobacteraceae; Glaciimonas.
OX NCBI_TaxID=2590999 {ECO:0000313|EMBL:MQR01339.1, ECO:0000313|Proteomes:UP000451565};
RN [1] {ECO:0000313|EMBL:MQR01339.1, ECO:0000313|Proteomes:UP000451565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS1 {ECO:0000313|EMBL:MQR01339.1,
RC ECO:0000313|Proteomes:UP000451565};
RA Wang L.-T., Shieh W.Y.;
RT "Glaciimonas soli sp. nov., a psychrophilic bacterium isolated from the
RT forest soil of a high elevation mountain in Taiwan.";
RL Submitted (OCT-2019) 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:MQR01339.1}.
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DR EMBL; WINI01000006; MQR01339.1; -; Genomic_DNA.
DR RefSeq; WP_153234966.1; NZ_WINI01000006.1.
DR OrthoDB; 9146932at2; -.
DR Proteomes; UP000451565; 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; cd00088; HPT; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR051315; Bact_Chemotaxis_CheA.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR058661; FimL_2nd.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR003594; HATPase_dom.
DR InterPro; IPR005467; His_kinase_dom.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF26379; FimL_2nd; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 3.
DR Pfam; PF00072; Response_reg; 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; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 4.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000451565};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 751..851
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1006..1109
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1199..1314
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1495..1692
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1694..1832
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1878..1994
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1402..1429
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 798
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1052
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1252
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1927
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2000 AA; 218992 MW; AF610E1E0D12F040 CRC64;
MTTAFSQPDT GPLSWVMNEI QEALTQSATA LQKLSSDQNK DQSTQLLLAK TYLHQAHGAL
QMVDISGVTI LTEAVEELLD QAQAAQTDEN SNVAVLSAEQ VATIGQTYQA LIAYLEELLA
GAAHQPVKLF PYYHALMQVV RTAAGQQKCH PADLFFPDLS IRPQFVVEGQ QNIELDLKSL
RKRFEMALLP FLKSSDSTVE CQNAAIMQSV IGEVEQAQTH QQSRAFWWVM NGFSDGVANA
DIVTNEGNAL HVKQLFARIN LQLRRLSEGS SSISERLLRD ALFFIAGIQT PSAKNQQIRL
AYRLEGAVPA DYQARHYDQV NPVALQAAKE HLTQAKNMWD NLASGNPAPA QNFEQQMHAL
SESGGQLNAP SLAKLLRELS GIARHAAYAK PGDAIGIEIA TSLLFIENTL SHIHRLPENF
SERADAMSAR LLSVMSGETP TEPAHWLGEI YQAAQQRQNV KTLAHEMLVS LRQVEKMLDE
YFSEPAKRTV LTRIDHVLSQ IQGALSILDH VESNADAAEV ITHTRATLQQ FSDAEDGQLP
EQIEFERIAQ NIGALSFYLE MLQHQSGHAD HQHCRLNFDE ERQVFRINLL ERTASTVVSE
PVVHVVAPAV PVSAIVPVAE NFAPLVSEAA TSGESASAAH DEFPALSFPH LPTIEEELLQ
HQQQAAELAI SLSNEPQNLE LQEQLKASLV QVRADARLSD DHSASDRAQA AIDLLAAPNA
TIAELVTAIV PAHTENHSPE ITLSAPMPTS EEEADAELQE IFLSEADEVC ACVHETLPEA
RLAPHNQEHL TVLRRAFHTL KGSSRMIGLT AFGEAAWSIE QVLNLWLSEA RNGTPSLYAL
LDEATQYFEG WIADIRAMGT SHRTAEALSA SAQQVRDGHE FLPAHVISAV LDTSDDAELN
AELSAELTDE VVSPAFIVQA TELQPSDIQL SEVSEDEFAD AIALFASEHT GTESPVVELA
SYAEHNVDAL QLPPDQPQHQ AESAEVIAFP GVPESRPDDS LKKIGELQIS LPLYNIYLTE
TDQLVRLLAR DFSEWRHEPE RVVAVQAIHA AHSLAGSSAT VGFKPLQELA HALEMLLQRA
ALQPTVMQEQ DFVMITLAVD QAKAMLQEFA QGEMPYYEPA LVSGLNALMH ANDEPRKDDD
AEVLQSLSPS SDNVQHLHVL ESVTAIAETE PMLIETMAPV VPRLFEQSTE ELDANLTLRD
DLDEDLLPVF IEEARDMLPQ IGGALRDWQQ SAQETSVAMP TAIIQAILRH LHTIKGSARM
AGAMVLGQHM HEMESQIEII SHSSDDQSKA EHILHKVEEL LAHYDHGVQL FEDLCSPQPK
PKAIAASAAS VTSTVAPVGA SSALTSVIVP KMAGLIAATT AATPLPVKAP VQQVRVNADI
LDRLVNQAGE VSIARSRLES GVGTLQSSLS ELDENVVRLR EQLREIEMQA ETQISSRMTQ
AGEREFDPLE FDRFTRLQEL TRMMAESVND VATLQKTLTK SADDASADLV AQGLLTRDLQ
QDLMHVRMVP FASVAERLYR LTRQVSKELD KRVTLDILGS TVEMDRGVLE KMVGPFEHLL
RNAIVHGIET RDERRLAGKS DVGELKIEIL QDGNEVLIQL TDDGQGLNLS RIREKAQSNG
LISTDLLLSD GEVTDLIFKP GFSTATEVTE LAGRGVGMDV VRSEATSLGG RVAVNTEAGK
GTTFAIHLPL TLAVTQVVIF STGGQTYAVP SALVEQVQQL KAPMLAQAYN EGTLLWQGQR
VPLHYLSALL GEHEAVPAAQ QYTPIVILKS GNSVNNRVAL HVDTIVGNRE VVVKNIGPQL
SRMIGIVGAT VLGSGDIVLI LNPVPLAQRF AQEVRAPRSG MTTETVHAVE GVGAVAEMEA
RVIAPTVKLE QGLRTQKIVM VVDDSLTVRR VTQRLLMRES YQVVLAKDGV DALQQLQAIT
PDVMLVDIEM PRMDGFDLTR NIRSDERTRH IPIIMITSRT ATKHRAYAME LGVNEYLGKP
YQEDALLSAI SGFMQKSIPA
//
