ID M0APR0_NATA1 Unreviewed; 1454 AA.
AC M0APR0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C481_12644 {ECO:0000313|EMBL:ELZ00495.1};
OS Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS P-10747 / NBRC 102637 / 172P1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=29540 {ECO:0000313|EMBL:ELZ00495.1, ECO:0000313|Proteomes:UP000011554};
RN [1] {ECO:0000313|EMBL:ELZ00495.1, ECO:0000313|Proteomes:UP000011554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12278 {ECO:0000313|EMBL:ELZ00495.1,
RC ECO:0000313|Proteomes:UP000011554};
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};
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:ELZ00495.1}.
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DR EMBL; AOIO01000030; ELZ00495.1; -; Genomic_DNA.
DR RefSeq; WP_006109568.1; NZ_AOIO01000030.1.
DR STRING; 29540.C481_12644; -.
DR PATRIC; fig|29540.5.peg.2562; -.
DR eggNOG; arCOG03730; Archaea.
DR eggNOG; arCOG04403; Archaea.
DR OrthoDB; 293137at2157; -.
DR Proteomes; UP000011554; 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: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 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELZ00495.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000011554};
KW Transferase {ECO:0000313|EMBL:ELZ00495.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1025..1234
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 325..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..582
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..654
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..830
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..904
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1320
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1454 AA; 152383 MW; 1189C5B700C53407 CRC64;
MTDYWSDFVR ESEDRITELN NALLTLERNP DDEAAMDKIF RIAHTLKGNC GAAGLESASN
LAHAIEDVLD AVRRNRLTVS PELMDAIFDA VDELERMVEE VALEGEIETD PSATIDSLRA
QLEPTAETDG LSSPSTAEIE RILSHFEPPA DDNHSAYLAR IEVADDGAKD DHEEIDNGIL
VVEALIDAFD LIGTDPDRST IADGAYGTTF DAVFGSAVGK GAIASGLDPV GEVADFELVD
VTTQFEDLVA DREETADTTT AEPGSQLSAD EAQELEVDDL LDEFTEFDDL DEKVEEVDDS
DLDVFDDMGD AGAFDDLLAD ADADVDDLDL GSPAPSEPSA TADAGVSTGA DPEPANGSTE
TDASDTADDS TTATETEQAS ATAAPDESDD VDDAEAVFAE LKDEVDTVGF DELQEELAEL
EFDEFDQEDE VGMDELLGDA ADADEPFLAG DSLNADEVES VSDAELDELV VADDASVSAD
DDGGETLASD AVGEESAGTD EPADAQERET DAGGVAESAS ASGSAATSGS ASECDAESDP
ETDAADGLAE SAESTESPEE AAESVADDTF EFDSETSVET DGADDTAPET ASAFEFESDA
ESTAATTQES ATESETTAET DTDPLNGSSI DDSETAAWFD ETDEADETVE PDEAASPATD
DPGVDADNAS AVDAESADRT QKSDAGIESN AEGDTGEFSE ADRGGELESD STVSTPTDDS
TDETVASEED ERIESGVETA ATEADDTADT TATTGFDAED SDASAFDESE PVAEASGFDS
QSGSTTPEFE PADADSDTTD IESGSDEEAG GDDEFSEVET DFDPAVTDDD VAFDDIDRAD
AADAEAFTSG LDTEVDDHSS TSRTETPAES ALGSDSATDD LDGFDGFDDD AFADLDESLE
SEPQTFESDF DSAAAVGTDS GFETTPESSA DGSDGGAVSS GESSATDSPR IDEPNLEIPE
ITVPETVERP DTDRETDEIQ SVRVDVEQID ELLTLVEGLV TSRVRLRHEV ESGQFGQSVA
DAGAITDELD DLEDLTTDLQ ETVMDVRLVP LRTVANRLPR VVRDIARDQG KTVAFEMSGE
DVELDRSILD RLRDPLIHLV RNAVDHGIES PEERDAADKP EEGTVEVSAS RSRDRVVITV
SDDGSGLDPE RLRSEAIEEG VLSADDAAEL DDESVADLVF HPGFSTTEEV TDVSGRGVGM
DVVKRTIEDL DGSVSIETDP SEGTTVTMSV PVSIAIDDVL FVESGGEEFG IPTKAVSDIV
PVELVEEVDG EAVLLDSAGS SESDRGVEVE SGAGDGAVEA DGDDVGSNDD TDATATDDDD
TDERTQERGT PVIRLGEELG VIDESAAGSE TDTSASTETS AGSAPDTATT GTRSGLAATG
SRDDRPGPRS PARGMVVRIR ENVRPIALRC DAVYGQQEVV VKPFEGFMAN LPGLSGATVR
GRGKIVNILD VTTL
//
