ID A0A0K2G6N9_NITMO Unreviewed; 956 AA.
AC A0A0K2G6N9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NITMOv2_0173 {ECO:0000313|EMBL:ALA56613.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA56613.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA56613.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA56613.1,
RC ECO:0000313|Proteomes:UP000069205};
RX PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA Nielsen P.H., Wagner M., Daims H.;
RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT from the genus Nitrospira.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(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};
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DR EMBL; CP011801; ALA56613.1; -; Genomic_DNA.
DR RefSeq; WP_053378077.1; NZ_CP011801.1.
DR AlphaFoldDB; A0A0K2G6N9; -.
DR STRING; 42253.NITMOv2_0173; -.
DR KEGG; nmv:NITMOv2_0173; -.
DR PATRIC; fig|42253.5.peg.170; -.
DR OrthoDB; 9783713at2; -.
DR Proteomes; UP000069205; Chromosome.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 2.
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; 4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ALA56613.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000069205};
KW Transferase {ECO:0000313|EMBL:ALA56613.1}.
FT DOMAIN 55..101
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 104..156
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 193..238
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 241..293
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 294..347
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 371..421
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 422..493
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 498..553
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 566..790
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 809..925
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 860
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 956 AA; 105155 MW; 4300F918F4A85AC1 CRC64;
MELNTVLLIG ALLLLGLSTW HGWHQRRDGV LKSKVIAAAS CGVAITDAAV PRHPVIYANP
AFRLLTGYAD EEVLGQSLSL LHGPQTDRVA IEKLALALQD GRPCRVVARH YRKNGAPFWN
EVTLSPVRNP LGEVTQFIWV MTDVTQRQQA EQSHKAPPNS SPASTLDTHL QSAQALAHVG
SWDWTIRDGT QVWSDEQYRI FGYEPGSVMP TYETFTAALH PDDRARVVAA VEKTLADGAP
YEVDCRIVQP SGTIRFVRCR GAVTRDAAGQ PVRMAGTVQD LTQYKLIESV AQEREAQFRL
AVESAPNGML MANQDGIISM VNGQIERLFG YTRDELLGRS VELLVPERFR SAHPDARRSF
FSVPATRAMG TGRELYGLRK DGTEFPLEIG LNPLETSSGR MVLAAIVDIT PRREAERTVR
ESQRRLDLAV EAAHVGIFEH DHRTDTLYWS PALREIYGLS ADEPGSLQRY LELIPQEDRG
AVLDALRQAH DPAGSGQFLV EHRLVRPDKS IRYVSVRSHT WFEGDGSARA PVRTIGAVVD
VTDLKQAEAS RRHASKMEAI GTLAGGIAHE FNNSLTAVLG FSELALPLIP ADSKAHRHIE
QVVAAGRKSR ELVHQLLTFS QQSDHVKRPL SLHTLVKESL KLLRPTIPAW IELRERIAAP
TRPISADTTH MHQLMLNLVE NALHAMRQSG GILDIRLEDR ELDVEQVSPS GRLAPGCYVC
LTIRDTGEGM DPEVVRRIFD PFFTTEPLGE GRGMGLSVVH SIVTAHGGTV LVESQVDVGT
TVSVYLPALP PRAAAPATAD VPPPHGHECI LFVDDEESLA RFGGEMLESL GYFPVVRMNA
ADAWQAFSIA PQRFDLLITD QCMPGMGGDL LAEECRRLRP DLPVILCTGS DQRRSAAEAR
VQGPAEYLLK PLALHDLAHA IRRLLDARDT GGSPRAAQTA VTLFVEEDAD AVSTRR
//
