ID A0A1E2WP03_9NOSO Unreviewed; 1263 AA.
AC A0A1E2WP03;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A4S05_04045 {ECO:0000313|EMBL:ODH00056.1};
OS Nostoc sp. KVJ20.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=457944 {ECO:0000313|EMBL:ODH00056.1, ECO:0000313|Proteomes:UP000094607};
RN [1] {ECO:0000313|EMBL:ODH00056.1, ECO:0000313|Proteomes:UP000094607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KVJ20 {ECO:0000313|EMBL:ODH00056.1,
RC ECO:0000313|Proteomes:UP000094607};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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:ODH00056.1}.
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DR EMBL; LSSA01000178; ODH00056.1; -; Genomic_DNA.
DR RefSeq; WP_069068541.1; NZ_KV757557.1.
DR AlphaFoldDB; A0A1E2WP03; -.
DR OrthoDB; 415806at2; -.
DR Proteomes; UP000094607; 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 CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
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; 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; IPR013655; PAS_fold_3.
DR InterPro; IPR016132; Phyto_chromo_attachment.
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; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..126
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 158..294
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 400..452
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 459..531
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 536..589
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 665..715
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 740..986
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1010..1123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1145..1261
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 884..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 706..740
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1059
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1194
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1263 AA; 141746 MW; 225C27435B583A3B CRC64;
MSHPSCLTIL LIDCAEDREA YCRFLKQDSV YTYRILELET ATQALKWCQQ EIPDIILLDF
VLPDGDGLKF IQQFWESYNH TQTAVIMLTA QGDEAIAVRA MKSGVQDYLV KDKLTAEVLQ
GAIHHAVERM HLTRQLEQSR EQQQLIAAIA LRIRQSLKLE EILHTTATEV RQFLKADRVV
VYQFQPDMSG TIVAESVLPG WTVALGREIL FTCFQQEAES DYRQGKKLAI DDIYQVELTN
YHLHILEQFE VKANLVVPIL VKEQLWGLLI VHQCSASRHW QSVELDLLDQ LAVQIAIAIQ
QGSVYQQAQA ELAERQRTEA ALKASEEKLK LTLNFTGIGY WELNPITNQI FASENTIYCF
GSDLSDANWT YEKWINQLYP EDREWVEMEL SQAIATQTDY AVEYRVVWQD GSIHWVSAKG
RGVYDATGQL LRMLGVLTDI TERKLSEQEL QRTQMLRIEL HLLEQILEVV LAGYWDWDIP
GNQEYLSLTF KQMFGYEDHE LPNTPESWQN LIFSEDLPGV LELFNRHIQS RGQIPFYNEV
RYRHKHGSTV WVICSGHVIT WDQDGNALRM IGCHIDITQR KQAEQELIHN QDLREAIFNE
SADAIFLVDP QTLLILDCNR RAVELFEAVD KAELLNINGQ RLQYRPFTAS ETDAIVTDMQ
SKGVWSREIE YVTLQGKIFW GNIAAKPITV AGRTMNLVRV TDISDRKQAE AQLRQTNEQL
ANANVELARA TRLKDEFLAN MSHELRTPLN AILGMSEGLQ ESVFGSINAR QVKAIATIER
SGRHLLELIN DILDLSKIES GKLELQLSDV SVRSLCDTSI AFVKQMALKK NIGLSIHISE
HIHSIQVDDR RLRQVLINLL SNAVKFTPDG GSVTLEVRVE GEGGRGAGGA GEAGEAGGVN
SSLSPSSSPN LCFHVTDTGI GIAAGEIGKL FQPFIQLDSS LNRQYSGTGL GLALVKKIVA
LHGGTVLVKS EVGEGSCFTV CIPYHTRDNV SITQATTLLP SHHLPAENAQ VLIIEDSVAA
ADQITRYFSE MGMQPIIYPK GEGAVEEVLR LQPALIILDL QLPNLSGWEV LNQLKTNPKT
KNIPAIIISV VDERSKGLAQ GAFEYLVKPI TRTQLQATID KLQHSAYSKP PNLIGVPEAV
LDTPLILLAE DNQANIDTMS GYLEGRGYHL ILANNGQQAI DLVRVQRPDL IVMDIQMPGM
DGLEAMRRIR NDQQFVHIPI IALTALAMPG DRKTCLAAGA NEYFTKPIKL KQLVTTIQEL
LSR
//
