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Database: UniProt
Entry: A0A2V2N908_9EURY
LinkDB: A0A2V2N908_9EURY
Original site: A0A2V2N908_9EURY 
ID   A0A2V2N908_9EURY        Unreviewed;      1000 AA.
AC   A0A2V2N908;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DK846_07500 {ECO:0000313|EMBL:PWR72787.1};
OS   Methanospirillum lacunae.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=668570 {ECO:0000313|EMBL:PWR72787.1, ECO:0000313|Proteomes:UP000245657};
RN   [1] {ECO:0000313|EMBL:PWR72787.1, ECO:0000313|Proteomes:UP000245657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ki8-1 {ECO:0000313|EMBL:PWR72787.1,
RC   ECO:0000313|Proteomes:UP000245657};
RA   Dueholm M.S., Nielsen P.H., Bakmann L.F., Otzen D.E.;
RT   "Draft genome of Methanospirillum lacunae Ki8-1.";
RL   Submitted (MAY-2018) 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:PWR72787.1}.
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DR   EMBL; QGMY01000006; PWR72787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V2N908; -.
DR   Proteomes; UP000245657; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   CDD; cd17909; CheC_ClassI; 1.
DR   CDD; cd16916; HATPase_CheA-like; 1.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 3.40.1550.10; CheC-like; 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; 2.
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; IPR007597; CheC.
DR   InterPro; IPR028976; CheC-like_sf.
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:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF04509; CheC; 2.
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; 2.
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; SSF103039; CheC-like; 1.
DR   SUPFAM; SSF50341; CheW-like; 1.
DR   SUPFAM; SSF55052; CheY-binding domain of CheA; 2.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245657};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..103
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          350..638
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          640..769
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          132..153
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   1000 AA;  109356 MW;  C01F5F88C9B9D431 CRC64;
     MSDLDAYRSL YVAESRENHE SIVSNLLILE QGTDSHAIDE IFRSAHSLKG MSASMGFMHM
     EEICHALEDV FSQIRSGNLH VSQALMDDLL AGVDDIESMI DDIEAGGEGL LEHRDARVSA
     LKAWLSGSSP STVEKKEPVI PDSGTEVEPA GDMYENPAYE SYDQAGNAEY KLHIELSSEV
     DSINLRSMLI LQNLESIGSI SAISPSRTVV EDDPSFNGII DLTFVTNAGK AAVETILAIS
     DIRSSSLSEE VSPQKKESVE PVPDFEHASR YAIHVELSPS VDSKNLRAML LLQNLESHGA
     LTNISPRREV IEDSGTFSGI FDFELTSSDF SEEGIKSFLK GSDIKSSSVS LIQDVSDPIL
     SGSGIEEHQN GTLAPSRISA GEKVEKKREV KNIRVDIDRL DHMMNLVEDL VINRGRLEQI
     AQEYKIKELD ETLNMVGRSV ADLQVMMMDI RMIPLNHIFN RFPRTVRDIA TKEGKEVDFI
     VEGGETELDR SVMDGLNDPL LHLIRNGLDH GIEPPDVRIR NGKNPKGTLK LSASRDKDNV
     VIVIEDDGAG INQEKIKKKA LERGLATEEA LAAMSESEIN DLLFLPGFST ADKITDISGR
     GVGLDVVRTT IASLQGTIKL ESVFGQGSRF ELVLPPTMAI VMVMMIRINN RRCAIPITNV
     AEVASLAAFP IQNIGHGEGI LMRDEIIVLY RLDDMFGRSK SEEVIVVLQN QNRKGAVIAD
     LIEGQQEVVI KPLSKFVGTC DGVSGVTIPG DGEVVPVLDV KAILREGSGQ KSAKKNSGKR
     VKKVMKNNVI ADGEHLITDI QADELRELGN IGASHAATTL STILNTLISI HVPEIILVQL
     QNLRYYLDDT EAAMVVFQIQ GQLVGNGYII IHIPKESIIR LTSIMLGQSA SDREIDDMDK
     SALHEIGNIM TSSFLDACAT LLSIIMIPSP PSMVIDMPHA ALQSIIATQE IDENVDEVVL
     FKTELQCAEY NISANIILLP SKGLLNELFA RMDSVISTSG
//
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