ID K9W2P3_9CYAN Unreviewed; 1600 AA.
AC K9W2P3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cri9333_3808 {ECO:0000313|EMBL:AFZ14618.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ14618.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ14618.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ14618.1,
RC ECO:0000313|Proteomes:UP000010472};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-2012) 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};
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DR EMBL; CP003620; AFZ14618.1; -; Genomic_DNA.
DR RefSeq; WP_015204718.1; NC_019753.1.
DR STRING; 1173022.Cri9333_3808; -.
DR KEGG; cep:Cri9333_3808; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_000445_114_15_3; -.
DR Proteomes; UP000010472; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 6.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 7.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; 7.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF01590; GAF; 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; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 7.
DR SMART; SM00091; PAS; 7.
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; 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); 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 6.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFZ14618.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010472};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..189
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 196..248
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 249..294
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 374..446
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 499..541
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 577..632
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 705..757
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 758..828
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 831..883
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 891..936
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1228..1445
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1480..1598
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 100..127
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1529
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1600 AA; 180949 MW; 27604B1A76537A54 CRC64;
MLRVIRDRTK PYIVTLGIVA SALSLTLLLK PLLGTTNLPL FYAAVSVSAW YGGMNAGLLA
TLLSTIAIQY FFIIPLHNFA INDLTHIVRL GVFVLVTLLI SSLNSELRAA KQRIEKSLIK
LKASEEQYRL IVDTAYEGIW KYNSDAETEF VNQRLAEMLG YTSEEMLGRK VFDFIDKDKR
EQVEQILQRR KQGIKEQYDF CFRCKDNSEL WAIVTSSPII DQNGESIGGI AMLTDVTERK
QAEFALKESE ARFRSIVESD MIGIAFWESD GSIKDPNAAF LNIIGYREAD FIDKKIRWQD
LTPAEYFHLD AIALTEIKNN RFCTPFEKEY IRKDGSRVPI LIGGCSFNGY TDKGAFFVLD
ITKRRLAEQA LRQSESRLKH LVDSNLIGII FADFNGNIIE ANDAWLNILG YTRSEVLSGK
INFLEITPPE YRHLDLQAIE EMKRTQKHTP FEKEYIRKDG SRIPVLVGTA YIPGDEGVGI
GFLIDLSERK QIEKAINESE NRFRTLIEQS PLSIQILASD GRTIKVNRAW EKLWGISIDK
IPEYNMLEDQ QLVEKGIMPY IKQAFAGEAV EIPAIKYDPN ESIPDRTINQ DPIRWVSAVA
YPVKNEDGSI REIVLIHEDM TARKRAEDAL QEREAELTLI TNAVPVLISY IDTEQRYRFN
NQKYEEWWGN SPTEIYGKHI QEVLGVAAYE RVFPYIKTVL SGQQVSFESE IYYHKMGKRY
VSITYVPQFG HNKEVKGFVA LISDLTERKQ AEDAIRESEE RFRIMADTAP VLIWMSGLDK
LCYYFNQRWL DFTGRTLEEE LGNGWAEIVH PEDLQRYLDI YTNSFDAHQE FQMEYRLKRF
DGEYRWVLNK GIPRFLPDGT FIGYIGSCAD ISDVYNELRL RKLAEAELQA TNQTLQALIK
ACPLAITVFD FNGIVKLWNP AAETIFGWSE QEAIGQFIPP VPEHKQQEFI ANLDAIKQGQ
QFIGLEARRQ TKSGVMIDVA LWAALLQDHQ GNLNCISIIA DITKRKQLEA ERTKLLELEQ
AARIVAVNEA ARSAAAQQRV AFLAEASRVL SSSLDYKTIL SSIADLVVPG IADFCFFDAV
TPENKIERVV WRHADPNKKE WFNQVQYYVP THDVKAHPVT SVLLTGKAQF IPEVSDEWFQ
KIAINSEHLQ FLRGLNSRSL ITVPIIAHDR ILGTLTFCVT PGFERSYTHD DLLLADDLAH
RAALALDNAS LYTEAQQANR MKDEFLATLS HELRTPLNAM VGWIQLLRTR TFDPQTSARA
LETIDRNTKS LAQLIEDVLD VSRIITGKLQ LKTHPIEIVP VIEAAIETVQ AAANAKYIKI
ECLLNSTEKV LGDPNRLQQV AWNLLSNAVK FTPQNGRVEV RLEQINNHVH IKVIDTGRGI
KSEFLPYVFE RFRQADNSIT RSYGGLGLGL AIVRHLVELH GGTVHVESEG EGKGATFVVI
LPAIAHNHNQ VKPETSTYNQ NIDLSPPPDS VSSSLLSGLH ILVVDDEPDA RELLIAILGD
YGAEVTAVSS AREAFELLQK LQPNVLVSDI GMPGEDGYTL IRKIRALHPE QGGKIPAIAL
TAYARTEDRN QAILAGFQLH ISKPVNPTEL ATMVANLLIN
//
