ID L0JPE0_NATP1 Unreviewed; 1182 AA.
AC L0JPE0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Natpe_2661 {ECO:0000313|EMBL:AGB32467.1};
GN ORFNames=C488_12423 {ECO:0000313|EMBL:ELY73607.1};
OS Natrinema pellirubrum (strain DSM 15624 / CIP 106293 / JCM 10476 / NCIMB
OS 786 / 157).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=797303 {ECO:0000313|EMBL:AGB32467.1, ECO:0000313|Proteomes:UP000010843};
RN [1] {ECO:0000313|Proteomes:UP000010843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 / JCM 10476 / NCIMB 786
RC {ECO:0000313|Proteomes:UP000010843};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGB32467.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 15624 {ECO:0000313|EMBL:AGB32467.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000011593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 {ECO:0000313|Proteomes:UP000011593};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ELY73607.1, ECO:0000313|Proteomes:UP000011593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 {ECO:0000313|EMBL:ELY73607.1,
RC ECO:0000313|Proteomes:UP000011593};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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; CP003372; AGB32467.1; -; Genomic_DNA.
DR EMBL; AOIE01000076; ELY73607.1; -; Genomic_DNA.
DR RefSeq; WP_006181853.1; NZ_AOIE01000076.1.
DR AlphaFoldDB; L0JPE0; -.
DR STRING; 797303.Natpe_2661; -.
DR GeneID; 14335824; -.
DR KEGG; npe:Natpe_2661; -.
DR PATRIC; fig|797303.5.peg.2503; -.
DR eggNOG; arCOG03730; Archaea.
DR eggNOG; arCOG04403; Archaea.
DR HOGENOM; CLU_262606_0_0_2; -.
DR OrthoDB; 293137at2157; -.
DR Proteomes; UP000010843; Chromosome.
DR Proteomes; UP000011593; 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: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; IPR010808; CheA_P2-bd.
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:SF10; 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; 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:0000313|EMBL:ELY73607.1};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AGB32467.1};
KW Nucleotide-binding {ECO:0000313|EMBL:ELY73607.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:AGB32467.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 846..1055
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1057..1182
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 310..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 836..863
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 347..362
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..595
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..618
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..749
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..777
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1182 AA; 125520 MW; B22CE4D8586201DE CRC64;
MTEYLTDFVQ ESEERITELN NALLTLERDP DDEEAMEEIF RIAHTLKGNC GAMGLESASD
LAHAIEDLLD AVRGGDIEVT PELMDVVFDA VDELETMIDE VAADGEIDTD PSATIDAVRE
YLERDTARPG LASPTPEEID EICSRFAPPT DDDRDVYLAR LDIAEREGVN NGKLVVDALI
DAFELMGTAP SRDRIEADEY DRGFDAVFAT AVGEAAIASG LEPVEEVDDF EIVDVDDRFE
AAPADDPGDV AAEDITSADA QDLEVDELLD EFNEFDNLDE MVEDVEDEEL DAFEDMGEAG
SFDDLLDEED VEELEAEPGQ PPAEHREPDA ASGGANADAA AGGSAADDGD DGDDEVDDAS
AVFDELKDEV EMVGFDELQD ELEELEFDEF DEDEEVDMDE LLGEEADDDA FLEGEEPTES
AVDDMLVDAE TEPAADELAA GESEVGGSAD AEETADTDVV AAPASDDRES GTESDEPATD
APETEPADGI EADTTAEPAD EPEATSDTAG SPASAEATAE SADTEAETAL EKSTEPDGTA
APDADDADDT EPGAAETDRP ADDPIVVDDA PADEAGVSDA DTEPAIDDAT DESVAVDADD
GAPTDLETET DDGTDLEEAD TATAGADTVD DVETDDGAET PAADSSVADA DIEAGTADDS
FGTDDGFEPS AGFDDGLETA DEDPFGDEPI DDAADSFGAD DEFEVSADSV DLEDGDDGFG
GFDDDIDDGL DDDAFDDTDA FDVDTDFGSS TDESESGSES SFGDDADDDE SDDVVRTVEE
PEFEIPDIEI PDTDVEQDAD DEADEIQSVR VDVEQVDSLL NLVEGLVTSR VRLRHAAEAN
DDNDALETEL DALSDLTTDL QETVMDIRLV PLRTVTNRLP RVVRDIAREQ DKEVAFEMTG
EDVELDRSIL DRIGDPLIHL VRNAVDHGVE PPAEREAADK PTEGSVEVHA DRESDRVTIT
VEDDGSGLDP DRLRDEAVEA GVLEPEVAAE LPDEDAYDLI FHPGLSTADE VTDVSGRGVG
MDVVKRTVED LEGMVSIDSE AGEGTTVTME LPVTVAIDEI LFVESGGEEF GVPTKAVRDI
EPASAIETTD GESILPGEDG DYPVVSLADI LETPAAGANG NGMVVRIRDD VREVALHCDR
VSGQQEVVVK PFEGFMSGVP GISGATVRGR GEVVNILDVT TL
//
