ID A0A1E7ZCV5_9ALTE Unreviewed; 904 AA.
AC A0A1E7ZCV5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BFC18_09300 {ECO:0000313|EMBL:OFC71338.1};
OS Alteromonas confluentis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1656094 {ECO:0000313|EMBL:OFC71338.1, ECO:0000313|Proteomes:UP000175691};
RN [1] {ECO:0000313|EMBL:OFC71338.1, ECO:0000313|Proteomes:UP000175691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42603 {ECO:0000313|EMBL:OFC71338.1,
RC ECO:0000313|Proteomes:UP000175691};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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:OFC71338.1}.
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DR EMBL; MDHN01000015; OFC71338.1; -; Genomic_DNA.
DR RefSeq; WP_070125025.1; NZ_MDHN01000015.1.
DR AlphaFoldDB; A0A1E7ZCV5; -.
DR STRING; 1656094.BFC18_09300; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000175691; 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; 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 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; 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:UP000175691};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 525..770
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 772..904
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 352..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..514
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 904 AA; 99232 MW; F0952251373D837E CRC64;
MSELLDTFIG ESRENLESAS QELITLQTNG YDAKAVDTIF RDIHTIKGSS DLFDIKPLTR
LAHASEDLLD CLRASEIPFS DELGDVLLES FDQISTFFDE LEAGTHQLSQ WEGVSAELAG
RLRNFMNTTD APSGNEATQP VENAVEAPAG IAAPVAALPE TAANWLSSMS DTARLTLFFK
SQESTRLHYF HYTPDADCFF RGEDPFNVSL ATPGFITHTI TRKSHVEGPE DVFLCHLDIL
LLSSADWDSL SSHFAYYEGQ YEHTQISAEQ VYQQCAPLIS QILNEEEVET LAQALENEGP
EQIARICNFV CASTNPDSAV WQFCAGIERL TENPAMLSAF CQCLFATPDT AQTEETPVAD
DVSEESIAEA APTQPAESEG LSENALAMLK QQETVLIRLI DGRGNQGALA SINLIVSRIL
NLDIVDRTPE DLLRVIASEG EQNDSQEAPD ATDIQAPAVA DTEAPVASEQ AAAIDDVSAS
ANKPVAEATQ AEPAEAKPEP VSETSAKPAE RQVPRTLKVN QEKIDYLMDL VGELTVAKNS
LPYLARQAEE DGGSRKLSKQ IKSHFTIVNR LTEELQSAVL QIRMVPVSHV FQRYPRLVRD
LARKLNKKIE LEMQGEDTEF DKNLIESLSE PLIHLLRNSI DHGIEAPADR LAAGKNESGC
IQLIATPQDD NVVIEIRDDG KGIDPAKIKM LAYQKGVITE SQLESINDEE ALQLIFAPGF
STSEQVSDLS GRGVGMDAVK TMVTQAGGHI EMQSEVGKGT QFRLVLPQTM SVNRVMMFEV
NEQMFGVSMD SVVETVKVRP DEIQQIKNHQ VLVIRDKLVP LHDLREYLGF ELQTQNVEEQ
SILVVNTGNG DMGLVIDKFH EGIDVIQKPL EGVMAGYSHF SGTALLGDGR VLLIVNVPEL
LSCR
//
