ID A0A1W9I004_9PROT Unreviewed; 2096 AA.
AC A0A1W9I004;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A4S14_16475 {ECO:0000313|EMBL:OQW52892.1};
OS Proteobacteria bacterium SG_bin9.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1827385 {ECO:0000313|EMBL:OQW52892.1, ECO:0000313|Proteomes:UP000192684};
RN [1] {ECO:0000313|EMBL:OQW52892.1, ECO:0000313|Proteomes:UP000192684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG_bin9 {ECO:0000313|EMBL:OQW52892.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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:OQW52892.1}.
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DR EMBL; LWDM01000080; OQW52892.1; -; Genomic_DNA.
DR STRING; 1827385.A4S14_16475; -.
DR Proteomes; UP000192684; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 11.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 8.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 10.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 12.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 4.
DR PROSITE; PS50885; HAMP; 12.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OQW52892.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 114..171
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 211..263
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 303..355
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 395..447
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 487..539
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 579..631
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 671..723
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 763..815
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 855..907
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 947..999
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1039..1091
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1131..1183
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1427..1660
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1709..1822
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1831..1947
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1977..2094
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1355..1417
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1758
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1880
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 2027
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2096 AA; 225782 MW; B8BD44F8F89830A3 CRC64;
MASRSRLSQE DLPQDTPPPV LNGKPDHRRE LLQALQTMRM GDFSVRMAGD YAGIEGKIAD
VFNEIVSANE RMAKQLERIG QVVGRDGRTR QRVSFGVPGG AWSEMETSVN SLIDDLLWPT
REVTRAVAAV AQGDLLQTVE LSVDGRPLKG EFLQSATIVN TMIKQLSVFT SEVTRVAREV
GTEGKLGGQA QVPEVTGVWK DLTESVNSMA NNLTAQVRNI SDVTIAVASG DLSKKITVDV
RGEILQLKEA INTMVDQLRS FASEVTRVAR EVGTDGKLGG QAIVPGVAGT WKDLTDSVNA
MCGNLTAQVR NIANVTTAVA RGDLSRKITV DVSGEILELK DTINTMVDQL NAFASEVTRV
AREVGTEGKL GGQAQVPGVA GTWKDLTDNV NFMASNLTAQ VRNIADVATA IAGGDLSKKI
TVNVSGEILQ LKETLNTMVD QLNSFAGEVT RVAREVGTEG RLGGQANVLG VAGTWKDLTD
SVNSMASNLT AQVRNIAEVT TAVAGGDLSK KITVDVRGEI LELKDTINTM VDQLNAFAGE
VTRVAREVGT EGKLGGQAVV RGVGGTWKDL TDNVNSMASN LTGQVRNIAE VATAVAQGNL
SKKITVNVSG EILQLKETLN TMVDQLNAFA GEVTRVAREV GTEGKLGGQA QVPGVAGTWK
DLTDNVNSMA GNLTGQVRNI AEVATAIAGG DLSRKITVDV RGEILQLKET LNTMVDQLNR
FAGEVTRVAR EVGTEGRLGG QANVPGVAGT WKDLTDSVNS MAGNLTAQVR NIAEVTTAVA
RGDLSRKITV DVKGEILELK NTINTMVDQL NAFAGEVTRV AREVGTEGKL GGQAEVPGVA
GTWKDLTDNV NFMASNLTAQ VRNIAEVATA IASGDLSKKI TVDVRGELLL LKETLNTTTE
QLRSFAAEVT RVAREVGTEG RLGGQAVVPG AAGTWKDLTD NVNLLAANLT TQVRNIAEVT
TAVARGDLSR KITVDVKGEI LELKNTINTM VDQLNAFAGE VTRVAREVGT EGLLGGQAQV
PGVAGTWKDL TDTVNVMAAN LTEQVRGIVK VVTAVANGDL KQNLTVKSKG EVAALAETIN
NMTDTLATFA DQVTTVAREV GVEGRLGGQA AVPGAAGTWK DLTGNVNLLA ANLTTQVRAI
AEVATAVTKG DLTRSIQVDA RGEVAELKDN VNTMIGNLRL TTDLNTEQDW LKTNLARFTN
MLQGQRDLAA VGRMLLTELT PLVNAQMGVI YRAESEETGT LRLLSAYAYD GAQPYPQLIQ
LGEGLIGQCA LDKRQRLISE IASNVVPINS ALLRVVPANV VVFPVLFENR VKAVIELASV
SAFTASQITF LEQLTDSIGI VLNSIEATMQ TEGLLKQSQQ LAGELQTQQR ELQQTNDQLE
QKAQQLAERN VEVEAKNQEI EQARRAVEEK ATELALTSKY KSEFLANMSH ELRTPLNSIL
ILGQQLSENP DGNLSERQIE FAKTIHGAGT DLLNLISDIL DLSKIESGTV TVEAEELYIS
NLLETVGRPF RHEAENRRLA FDVDIDTNLA RSMTTDSKRL QQVLKNLLSN AFKFTDQGGV
KLRVSNAASG WSAEHPVLNQ ASSVVAFEVS DTGIGIPVEK QRIIFEAFQQ ADAGTSRKYG
GTGLGLAISR ELASLLGGEI HLRSTPGKGS TFVLYLPIKY EGPSVNVRPQ AMAMASEAMP
VVSLVPSQER TPAESLLDDR LEVEPGDAIL LIVEDDLHYA RVLLDLARDK GFKVLVAMRG
ADALELAKQF QPTAVSLDVF LPDMLGWTVL SQLKHNPLTR HIPVQIITLD EDRQHALARG
AFAFVSKPTT MEGVSAALDQ IKEYARPRRK RLLLVEDNPA EQLSIQELLG HSDIEIVTAA
TGTEALSQLR LKETDCVVLD LRLPDMSGFE VLNRIREDKS LANVPVVVFT GRELSVEEDA
ELHTMARSIV VKGVESPERL LDETSLFLHR VITDLPPDKQ RMLEKLNGSD EDLVGQTVLL
VDDDARNIFA LSSVLERRGM KVLTATTGAD AITLVSENPS ISIVLMDIMM PQMDGYQTIG
FIREDKRFRK LPIIALTAKA MKGDREKCLE AGASDYLAKP VNTEQLLLAI RMWLHR
//
