ID M1X0P3_9NOST Unreviewed; 680 AA.
AC M1X0P3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RINTHH_14580 {ECO:0000313|EMBL:CCH67613.1};
OS Richelia intracellularis HH01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Richelia.
OX NCBI_TaxID=1165094 {ECO:0000313|EMBL:CCH67613.1, ECO:0000313|Proteomes:UP000053051};
RN [1] {ECO:0000313|EMBL:CCH67613.1, ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|EMBL:CCH67613.1,
RC ECO:0000313|Proteomes:UP000053051};
RA Hilton J.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|Proteomes:UP000053051};
RA Hilton J.A., Foster R.A., Tripp H.J., Carter B.J., Zehr J.P.,
RA Villareal T.A.;
RT "Diatom-associated endosymboitic cyanobacterium lacks core nitrogen
RT metabolism enzymes.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:CCH67613.1}.
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DR EMBL; CAIY01000052; CCH67613.1; -; Genomic_DNA.
DR RefSeq; WP_008234410.1; NZ_CAIY01000052.1.
DR AlphaFoldDB; M1X0P3; -.
DR STRING; 1165094.RINTHH_14580; -.
DR OrthoDB; 9788063at2; -.
DR Proteomes; UP000053051; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 2.
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; 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; 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; 2.
DR SMART; SM00091; PAS; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 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}; Reference proteome {ECO:0000313|Proteomes:UP000053051}.
FT DOMAIN 51..96
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 178..249
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 251..303
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 316..541
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 560..676
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 611
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 680 AA; 76952 MW; 9AB2AAAEB78D0EA8 CRC64;
MKIQSLYTSG DICGFRKNNQ CLHENNSLLE QDTKSNSLSN RIYDNSQTKI NILFLAEILD
LINDAVIITD TEYKVTYWNH KAEKLYGIKT TEIIGEILTV AFEPLWSYSQ QQQAYTDALE
QYGFWKGENI HLKKNGEKIY VDSSIFVLEE KFCGFLWIIK DLDNIYYERS LRQIAEYKVK
EQSTLIDFTR DAILMLNFDG EIIFCNEGGY RTYGWESSQM HGKNIRQILY DDSSLPQIEF
ALNKVLENGE WYGELYHLCK NGQKIILEAR WILIRDNQDN PQSILTAATD ITEKKQLETQ
FLRTQRLQSI GSLATGIAHD LNNILTPILA VAQLLPLKLP CINENTKGLL NIVLDNCKRG
SDLIKQILVF ARGAETQYMN LQVGHILVEV ARVIRQTFPK SMEICMDIST RELWMVFADA
TQLHQVLMNL CLNARDAMAN GGTLTLAIGN FFIDENHAGI HLDANVGPYV VVTISDTGCG
IQTENLGRIF EPFFTTKELG KGTGLGLSTV LGIIKSHGGF VDVCSEVDRG TCFKIYLPAV
ESIEKVEFSE LEPTQGIEEL ILVVDDEKTI LEMTKTSLEA YNYRVLIAKD GIEAITLLSQ
HEYKIKAVLI DFIMPILDTK ITISTLKKIN PQVPIIIMSG LASDEVITKT SSSDFQAFLA
KPFTTWELLS TLKQVINQSK
//
