ID A0A1M6N6H3_9CLOT Unreviewed; 673 AA.
AC A0A1M6N6H3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=SAMN02745912_01596 {ECO:0000313|EMBL:SHJ91318.1};
OS Paramaledivibacter caminithermalis DSM 15212.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Paramaledivibacter.
OX NCBI_TaxID=1121301 {ECO:0000313|EMBL:SHJ91318.1, ECO:0000313|Proteomes:UP000184465};
RN [1] {ECO:0000313|EMBL:SHJ91318.1, ECO:0000313|Proteomes:UP000184465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15212 {ECO:0000313|EMBL:SHJ91318.1,
RC ECO:0000313|Proteomes:UP000184465};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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};
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DR EMBL; FRAG01000015; SHJ91318.1; -; Genomic_DNA.
DR RefSeq; WP_073148699.1; NZ_FRAG01000015.1.
DR AlphaFoldDB; A0A1M6N6H3; -.
DR STRING; 1121301.SAMN02745912_01596; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000184465; 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 Kinase {ECO:0000313|EMBL:SHJ91318.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000184465};
KW Transferase {ECO:0000313|EMBL:SHJ91318.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 292..542
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 544..673
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 262..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 673 AA; 76179 MW; 987663762170FDDF CRC64;
MDMNQYLDIF IEESKEHLQD MNQLLLKLEA STDDLSLLNE IFRIAHTLKG MSGTMGYVKM
ANLTHEMENV LQSIRNKEIE ANEHIIDVLF ECFDTLEEYV NGLIKNGVEG DLDPKPLIKK
LSNIMNNNSM EKSHDEEDIK DEENNSKFTI DIEDITYNII NKARESNFSS FKIMVVLNPE
CMLKAARAFI VFNTLEKFGE IIRSKPSAEE IEDEKFDNAF EIIYITKLDE NTIRNEILNI
SEINEVVVER IKVEGNINKP QKIKETKKIN KPVSKNNDKP KKEEKSNKLK SKTSKTVRVD
IDRLDNLMNL VSELIIIKTR LEDIEDSKLN TNMNEAVEYL ERITTSLHDA VMKVRMVPIE
RTFNRFPRMV RDLSKELGKE IKLYMTGEET EVDRTVIDEI GDPLIHLLRN SIDHGIEDPK
TREELGKPKA GNVYLRAYPD GNNVVIEVED DGSGISIEKV RDKALSKGLV SKETIANMNN
DEIVNLLFKP GFSTAEKISD ISGRGVGLDV VKTKIESLGG LVEVHSEMNM GSKFIIRLPL
TLAIIQALMV TIGDEKYALP LNSIKEIATI KTNTIRKVHN QEVVLFRNNT LPILRMNEIL
QVNKISEDKD EMIIVVVKKG DKIAGLVVDN LIGQQEVVIK SLGKYLSGIK VIAGATILGN
GQIALIVDPN SLF
//
