ID A0A0N0VN35_9BACI Unreviewed; 677 AA.
AC A0A0N0VN35;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AAV98_12565 {ECO:0000313|EMBL:KPB04384.1};
OS Bacillus sp. CHD6a.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1643452 {ECO:0000313|EMBL:KPB04384.1, ECO:0000313|Proteomes:UP000037908};
RN [1] {ECO:0000313|EMBL:KPB04384.1, ECO:0000313|Proteomes:UP000037908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHD6a {ECO:0000313|EMBL:KPB04384.1,
RC ECO:0000313|Proteomes:UP000037908};
RA Lin W., Liu Y., Zheng Q., Jiao N.;
RT "Genome sequence of Bacillus sp. CHD6a isolated from the shallow-sea
RT hydrothermal environment.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KPB04384.1}.
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DR EMBL; LBMD01000014; KPB04384.1; -; Genomic_DNA.
DR RefSeq; WP_060665916.1; NZ_LBMD01000014.1.
DR AlphaFoldDB; A0A0N0VN35; -.
DR STRING; 1643452.AAV98_12565; -.
DR PATRIC; fig|1643452.3.peg.1363; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000037908; 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 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..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 294..544
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 546..677
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 677 AA; 75452 MW; 86E3C0DC6E287700 CRC64;
MDLNQYLDIF LEESKEHLQT INNQLLELEK HPANIEIVNE IFRSAHTLKG MSATMGYEDL
ASLTHQMENV LDLIRNAKLT VTTNLLDIVF RSVEYLEEMV LSISEGGDGK KDVSEVVSLL
VKIEKGEECS LPTKSADQTT SEHSYDSYEV TILQQSEEQG YTPYEVTVTL RQDCLLKAAR
VFMVFEVVEG MGEVIKSYPS VDLLEEEKFE DSFQITMVTK EEVSTIKEKI MKVSELEKVT
VNKLDTQLLA AFEAESFVEV AIEEVSTAQV EVATTTAVLE KKEDKPTPVK ATPGSNKTIR
VSIDRLDGLM NLFEELVIDR GRLEQISKDL NEPELIETVE RMSRISNDLQ NIILNMRMVP
IETVFNRFPR MVRQLARDLG KKVDIDIIGA ETELDRTVMD EIGDPLVHLL RNAIDHGIET
PEVRNRNGKP EEGRITLKAY HSGNHVFIEI MDNGAGIAKE KVLNKAISKG VISQQEGERL
TEQEVYQLIL SSGFSTAEVI SDISGRGVGL DVVKNTIESL GGKITIDSVE GAGTTFSIQL
PLTLSIISVL LTEVENEKYA IPLSSIIETA IIKKEEILTA HNQEVIDFRG KIVPVVYLEK
VFQVQKEQVE RPDFYSLVLV KKGEKIAALV VDSFIGQQEV VLKGLGQYLN STFAISGATI
LGDGQVALIV DCNALIK
//