ID A0A0K2GFP7_NITMO Unreviewed; 667 AA.
AC A0A0K2GFP7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NITMOv2_3002 {ECO:0000313|EMBL:ALA59407.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA59407.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA59407.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA59407.1,
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};
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; CP011801; ALA59407.1; -; Genomic_DNA.
DR RefSeq; WP_053380423.1; NZ_CP011801.1.
DR AlphaFoldDB; A0A0K2GFP7; -.
DR STRING; 42253.NITMOv2_3002; -.
DR KEGG; nmv:NITMOv2_3002; -.
DR PATRIC; fig|42253.5.peg.2965; -.
DR OrthoDB; 9784397at2; -.
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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:ALA59407.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000069205};
KW Transferase {ECO:0000313|EMBL:ALA59407.1}.
FT DOMAIN 254..301
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 315..359
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 386..440
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 453..665
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 667 AA; 73285 MW; 3EFBAF4E65FC1D23 CRC64;
MSKTLPPAPA VERPSLQETF VSYLAVWVGE SLRGGVGVVM NGALVFEDQR WRDLVGDEPG
GSRQTGDAGE AEELPQATRA GLLREALQIA AEPVGTRRTC RYRSRGTDQL RRLIEATVTV
VPLPEGNAVL VVLEDITERT CLAAEAATVG RFQSLLARIG ALAVSGTPVQ EIMHEAVRLT
AEALNVELVK ILIPRESDEH LYLIAGIGWR DGLIGSLTVE GGTHSQAGFA IRERQPVVVR
DLRAETRFTP STLLAEHGGV AGMSVPMMVQ DRVYGVMGAH CKSVREFSPK ELEFLCSVAN
TIATVLERWR REETQIQLYH RLFELVQDGV MLTDTNGRLL EWNPAMERMA GWTRAEVLGW
TPAILKSGKH SPEFYERIWQ AVRAGTPFTD RIINRRKDGS EFLAWESISP VKDPDGTIRY
VLAILTDLTE RERMLEALRH TEQVKLVGQL AGGILHEIRN PLIGIGSLAT HLAEQAALPE
SVRGRCRLIA EEASRIDAIL QSHLGQLPKR SFEFRPCDLP ALLEDTRALL QNKLEATRVA
VVTDLSPAVP SVEASRGHLQ QVWLNVMMNA IEVMPQGGQL TVRAHPATLR GEPGVIVVFE
DSGPGIAPED LAHIHEPFFT SGKAKGVGLG LTISRDIIER HGGQFTIKSP PGHGAIVEIW
LPVRQKE
//