ID G2IKL3_SPHSK Unreviewed; 807 AA.
AC G2IKL3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:BAK65076.1};
GN ORFNames=SLG_04010 {ECO:0000313|EMBL:BAK65076.1};
OS Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=627192 {ECO:0000313|EMBL:BAK65076.1, ECO:0000313|Proteomes:UP000001275};
RN [1] {ECO:0000313|EMBL:BAK65076.1, ECO:0000313|Proteomes:UP000001275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6 {ECO:0000313|Proteomes:UP000001275};
RX PubMed=22207743; DOI=10.1128/JB.06254-11;
RA Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA Yamazaki S., Fujita N.;
RT "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT lignin-derived biaryls and monoaryls.";
RL J. Bacteriol. 194:534-535(2012).
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};
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DR EMBL; AP012222; BAK65076.1; -; Genomic_DNA.
DR RefSeq; WP_014074728.1; NC_015976.1.
DR AlphaFoldDB; G2IKL3; -.
DR STRING; 627192.SLG_04010; -.
DR KEGG; ssy:SLG_04010; -.
DR eggNOG; COG0643; Bacteria.
DR HOGENOM; CLU_000650_5_2_5; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000001275; Chromosome.
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 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:UP000001275};
KW Transferase {ECO:0000313|EMBL:BAK65076.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 167..418
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 420..556
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 136..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 807 AA; 86517 MW; 8D89F676D4BC5787 CRC64;
MDEILAEFIA ETLETLETLS GEIVAWEADP TDRSRLDAFF RFFHTVKGSC GFLNLPRFER
LAHGAEDVLA AVRRGERVAD PATVSAVLAV MDRIGALARG IGEDVQIPDS EDDALLDALS
ISSGGFEIFE PLPEIASEPD GEERGTDPAP APEPLARRSS DGGNRDRAPR TIRLPLALID
QLMNGISDMV LARNDLARKM RDHGVDADLE SSFERLSANV ADLRDMISKT RMQRVDRLYA
AIPRMVRDLT RELGKKAVLS LDGGDVEMDR EMVEMVVDPL THIVRNALDH GIEAPAARLA
AGKPEAGALR IVARQSGNQI VIEISDDGRG INRAALVEKA VAAGLCTAVE AATLSDAEKL
GLIFHPGLST AASVTSVSGR GVGMDVVRAN IEQIGGVIGI TSLPGQGTTI TMRVPLTLTI
IPGLIVRCGE HFFAMPRGNV VELLHQNSSM VSIEAVGGAR IATIRGEHYS LVELEDILGL
PRVEGSGPRT LMVIRSSLGQ PYVLGVQSVE SNEELVIRPA SPAITAAGVF AGMTLPDNGQ
PMLLLDAAGL AQVAELPLRE AELRTRSAPA AAMADTREET IQALVFRERD GTTRLLPLAV
VDRVEDLEAS RITASNGRAF ARIEDRLLPA LNTQGEESGL PKSLRLHDGR DQICYLIEDV
IDIIEVPATL DVPIGAGRIA GLVMVGESQL EMIDPFALFA DAARTRQAAA AGQPIRCLIA
DAEDPWLRNI LAPLLIRAGH DVRFGPQAES PDVILCGDSP PDDPAGDVPV LMLRDVAEDT
SDAHASIYRY DREKIMAAIV EAARRAA
//
