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Database: UniProt
Entry: A0A0D6KLJ9_9CYAN
LinkDB: A0A0D6KLJ9_9CYAN
Original site: A0A0D6KLJ9_9CYAN 
ID   A0A0D6KLJ9_9CYAN        Unreviewed;       842 AA.
AC   A0A0D6KLJ9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-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=FDUTEX481_08782 {ECO:0000313|EMBL:EKF00635.1};
OS   Tolypothrix sp. PCC 7601.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF00635.1, ECO:0000313|Proteomes:UP000032761};
RN   [1] {ECO:0000313|EMBL:EKF00635.1, ECO:0000313|Proteomes:UP000032761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX   PubMed=25953173;
RA   Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA   Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA   Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA   Kehoe D.M., Weinstock G.M.;
RT   "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT   Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT   PCC 7601.";
RL   Genome Announc. 3:0-0(2015).
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:EKF00635.1}.
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DR   EMBL; AGCR01000054; EKF00635.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D6KLJ9; -.
DR   STRING; 1188.FDUTEX481_08782; -.
DR   PATRIC; fig|1188.3.peg.5803; -.
DR   HOGENOM; CLU_000445_114_51_3; -.
DR   Proteomes; UP000032761; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; cd00082; HisKA; 1.
DR   CDD; cd19410; HK9-like_sensor; 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; IPR007891; CHASE3.
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; IPR013656; PAS_4.
DR   InterPro; IPR013767; PAS_fold.
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:SF46; C4-DICARBOXYLATE TRANSPORT SENSOR PROTEIN DCTB; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08448; PAS_4; 1.
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; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:EKF00635.1}; Membrane {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:UP000032761};
KW   Transferase {ECO:0000313|EMBL:EKF00635.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        183..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          294..346
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          343..413
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          415..467
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          480..702
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          722..838
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         773
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   842 AA;  94220 MW;  72A6161D16FA51D0 CRC64;
     MMKWSVIQKL KAVFILVLAV LFTNAVVSHS TTMQLVQNWQ LITHSQEIIT QVQTLLTTLN
     NAETAQRNYL ITISTNNLVT YLQASQQINN NIQILKQLTQ AQQNHQWVAV LEQKITDRLN
     ILQAEVVVLQ NQGFDTARQS VLSHQQEMLS HDIPRFIHES LASEQKILQQ RNQQLQVTSR
     KSMATFLLAA IIDFLLVALL YDLLWCYIKR LQQTELNLRQ SENRLRAIID AEPECLKLIA
     KDGTLLEINA SGLAMLELES AENLIGQAFT ATILPEYREA FVSLHERVCQ GYKGNLEYEI
     VGSQGTRRWL ETHAVPLHNE ADGTFLHLAV TRDITKRQQA EQKIREQAAL LDVATDAIVV
     RNIHNQILFW NQGAEGVYGW KAEEVLGKNV VDLLYKDSSP QLEDAFLTVL RAGEWRGELQ
     QLTKQGKEII VESRWTLMRD SQNQPKSILS VSTEITQKKQ LEAQLLRSQR LESIGTLAGG
     IAHDLNNVLA PVLMSVELLR MKLPDQQSQR ILQTLESNVK RGANLLKQVL SFARGIEGKK
     TIVQTRLLIQ EIEQIIQQTF PKSITCQVDL SASLWYVFGN TTELHQVLMN LVVNARDAMP
     DGGILKISAE NVVIDEKSTL INIDAQIGAY IAISVRDTGT GIPPEIQERI FEPFFTTKEV
     GKGTGLGLST AIGIIKNHNG FVNVNSKVNQ GTEFQVYLPA FSNSTQPLHT PEIAAPTGNG
     EWILLVDDEA AIREITKSSL EKHNYQVLTA SNGIEAVAIY AQYQQQISVV LLDMMMPVMD
     GAIAIRKLQT INPHVKIIAL SGLLSPQNIK EVTDMGVSAF LSKPCTSNEL LQTIARIKVL
     GC
//
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