ID B2IZ13_NOSP7 Unreviewed; 989 AA.
AC B2IZ13;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Npun_R4769 {ECO:0000313|EMBL:ACC83120.1};
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC83120.1, ECO:0000313|Proteomes:UP000001191};
RN [1] {ECO:0000313|Proteomes:UP000001191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACC83120.1, ECO:0000313|Proteomes:UP000001191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RX PubMed=23463784; DOI=10.1104/pp.112.213116;
RA Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.;
RT "A Nostoc punctiforme Sugar Transporter Necessary to Establish a
RT Cyanobacterium-Plant Symbiosis.";
RL Plant Physiol. 161:1984-1992(2013).
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; CP001037; ACC83120.1; -; Genomic_DNA.
DR AlphaFoldDB; B2IZ13; -.
DR STRING; 63737.Npun_R4769; -.
DR EnsemblBacteria; ACC83120; ACC83120; Npun_R4769.
DR KEGG; npu:Npun_R4769; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_71_3; -.
DR OrthoDB; 442759at2; -.
DR PhylomeDB; B2IZ13; -.
DR Proteomes; UP000001191; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.250.690; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
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; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF00486; Trans_reg_C; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU01091};
KW Membrane {ECO:0000256|ARBA:ARBA00022519};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001191}.
FT DOMAIN 2..116
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 124..223
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|PROSITE:PS51755"
FT DOMAIN 397..513
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 592..645
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 670..720
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 724..941
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DNA_BIND 124..223
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT REGION 229..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 554..595
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 446
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 989 AA; 109638 MW; 1F24286FDDE1A04A CRC64;
MKILIVEDDG LNAYTLTNLL TNQNYAVEVA TDGDAAWDCI QAYDYDLILL DVVLPKLDGI
SLCRKIRSNN LQMPILLMTG RNSSHEKAIG LDAGADDYLV KPFDIEELVA RIRALLRRPA
VTSPPVLESG KLRLDPSSCE AVYARNLLPL TPKEFALLEL FLRNSRRVFS CGMILEHLWS
YEDTPQEEAV RTHIKGLRQK LKAVGAPGDL VETVYGIGYR LKPLEEDKHR GAGAGEQGSR
GAEEQGSRGE VDRVKSPIPN LKSQQQALMA VAEIWQRFQG RVEQQVRVLE QAIATLNQNN
SLNPELLSLA AKEAHTLAGS LGTFGLPLGS KWARNIELLL SYDQTLSKSE IGNLQIWVNL
LRREIEGNDA GAISGSSISQ VETVTQPLQN HPDAETKILV VDDDPQIQAL LQTLLSPWGL
RAIALENPLQ FWETLEAVAP DMLILDVELP YINGIELCRL VRNDSHWSEL PILFLTVHSD
AEMVNQVFSI GADDFVSKPI VGPELVTRIV NRLERMKLRQ RVTQGSRGAG EQGSRGAGGA
EEVNSPPSFS HRAINELELR VAERTAELIS VNQQLQSQLD ERQQTQEELR FSQARFARIL
DIADDAIISI NGFHNITLFN QGAEKIFGYC AQEVIGQGLD LLLPQRFFQA HRQHVADFGQ
SPNVARRMGE RREIYGRRKD GSEFPAEASI SKIDMGDEIF YTVILRDVTE RKQIERMKDE
FVSVVSHELR TPLTSIYGSL GMLASGLLPT DSEQGKRLLQ IAADSTERLV RLINDILDIE
RIESGKAKME AEICNIVDLI TQAVNVIQPL ADKAGVTLSI SALSGQVLAD CDRIVQTLTN
LLSNAIKFSS AGSTVWLGAQ QEGDEVLLTI KDTGRGIPTD KLESIFERFQ QVDSSDSRNH
DGTGLGLAIC KSIMQQHGGR IWAESILGEG STFYVTLPLF GTFPHTDLQN SSNIPVIYSR
HDQIINSHAS QDAEFLTKGR ITPRNLNND
//
