ID A0A0S8DJG6_9BACT Unreviewed; 783 AA.
AC A0A0S8DJG6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMK70_02580 {ECO:0000313|EMBL:KPK36361.1};
OS Nitrospira bacterium SG8_35_1.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704024 {ECO:0000313|EMBL:KPK36361.1, ECO:0000313|Proteomes:UP000052010};
RN [1] {ECO:0000313|EMBL:KPK36361.1, ECO:0000313|Proteomes:UP000052010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_35_1 {ECO:0000313|EMBL:KPK36361.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK36361.1}.
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DR EMBL; LJTK01000025; KPK36361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DJG6; -.
DR PATRIC; fig|1704024.3.peg.2699; -.
DR Proteomes; UP000052010; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 159..230
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 287..357
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 428..644
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 664..778
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 713
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 783 AA; 87932 MW; 4C1762D22D9E0003 CRC64;
MASPQTFSDI LGAGYKESVV ILSRDLKIIS ANETFLQDNN LSLQDIEGKT CHEVLQSCMN
FCKEQTDECP VYEALSTHRP VSVTQQDVMV DNKPHHYKID IYPVFGEKEA DTYFLHIARD
ITNRIEEERL KDNMWMEILS RMESLYAAMV QGNENIDLIQ REIDQLIEIV PLAVVGWDPN
GKINRWNSNA EILFGRPALE VIGKPFIDFF ASGKSQEKFS EIMHMLQMGQ TEVYSLAENR
TASGHIITCE WYHNAYQFNE KGDISAGLSI GQDASERLAT EKKVRKLENQ FAAILNATGD
AIVGMNNLRR ITLWNPAAEK LFGWLAREVQ GREIEMLIPS EQRESITRRF RKFFEEQEQK
KGQKTTFEIS ALRRDGITIP VEMTLSSAFI EGKISGFAVF HEITEKKRTE KILVQSEKMR
ALGEMASGVA HDFNNSLTTI LGNIKLLKEA GVDRNITDKI DAIEKAARQG AQTIASLQGF
STTADEDSHK PVKLLALKPL IEEVRNLTRF RWKDLPQKEG HTIEFTTEIE GSSALVINGA
DFKEMLTNLI FNAVDAMPQG GHIHLSVKQE DEKVVLAIQD NGVGLSKEDA AHIFDPYFTT
KGRGHAGLGL SIAKRFIERH GGSIRVESIK GAGSTFKVEF PLLTTSEPEK LVLSVRPKAP
VHLKILIIDD EPLVRSLLKQ VLEKSGHSVA EAGNGQEGIR SFRENNFDLV ITDHGMPVMN
GLDAAFRIKK QKPETPVLLI TGWQAETDAT FQKPSGIDEV ITKPFDLENL LDLVQLYGRK
IKK
//
