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Database: UniProt
Entry: K9WLU8_9CYAN
LinkDB: K9WLU8_9CYAN
Original site: K9WLU8_9CYAN 
ID   K9WLU8_9CYAN            Unreviewed;       667 AA.
AC   K9WLU8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Mic7113_4839 {ECO:0000313|EMBL:AFZ20507.1};
OS   Allocoleopsis franciscana PCC 7113.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX   NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ20507.1, ECO:0000313|Proteomes:UP000010471};
RN   [1] {ECO:0000313|EMBL:AFZ20507.1, ECO:0000313|Proteomes:UP000010471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ20507.1,
RC   ECO:0000313|Proteomes:UP000010471};
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., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003630; AFZ20507.1; -; Genomic_DNA.
DR   RefSeq; WP_015184642.1; NC_019738.1.
DR   AlphaFoldDB; K9WLU8; -.
DR   STRING; 1173027.Mic7113_4839; -.
DR   KEGG; mic:Mic7113_4839; -.
DR   PATRIC; fig|1173027.3.peg.5366; -.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3447; Bacteria.
DR   HOGENOM; CLU_411502_0_0_3; -.
DR   OrthoDB; 5555607at2; -.
DR   Proteomes; UP000010471; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; 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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR007895; MASE1.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF05231; MASE1; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFZ20507.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW   Transferase {ECO:0000313|EMBL:AFZ20507.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        50..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        208..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          401..652
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          339..380
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   667 AA;  73443 MW;  0AB39EFD9DFA8130 CRC64;
     MPRKLNSIVF VPQRWWLILP LGLLVLLLAH GMALIYRIQP AVSLWFPPSG VAIALTLWFG
     PVGVLLTAVS SILIAPQWGN EGWTQIMALT DATEPLVAWF LYRRCFMATL SLSTLRDAVA
     FTLSAPLAAC ATSAFVGSFA LVFVGKMPLS GLDRSILHWW LGNALGTLAI APTALLVLTP
     CLQRWGWLSL PHPANEPHLV RDCQSRRFWV EVVTIMLLTI ATAALTVSKS NNAGFVFQQF
     SFLSFIPMLW AATRFGVTGG MLTSSFCVLV TLLAYLLTYP DAISLPSFPL PAEVLSVHKL
     SLLVQCAVSL LVGCATTQQS KTQVALAVEG VRVLEHQARA QLNEQLLQLN SELQKANTRL
     EESNREKDEL LSREQIARAD SEAAQKAAEA ANRLKDEFLA VLSHELRTPL NPILGWSNVL
     RTRQCNEATT ERALVTIERN AKLLTQLIED LLDVSRILQG KLSLNVSPVN LVSTIEAAID
     TVYLAAQAKS IQIQTFFDPK VGQVLGDSNR LQQVIWNLLS NAIKFTPEGG KVEVRLSVVT
     RLKVNQLNVE SREDHLVYDF ANTVQPANIQ PSTSYAQIQV SDTGQGINPD FLPHVFEHFR
     QEDSTTTRVF GGLGLGLAIV RHLVELHGGT VYAKSSREGL GATFTVTLPL IFERPFNSEE
     NNNHSHN
//
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