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Database: UniProt
Entry: A0A3R9FP12_9VIBR
LinkDB: A0A3R9FP12_9VIBR
Original site: A0A3R9FP12_9VIBR 
ID   A0A3R9FP12_9VIBR        Unreviewed;       900 AA.
AC   A0A3R9FP12;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=EJA03_03250 {ECO:0000313|EMBL:RSD32488.1};
OS   Vibrio pectenicida.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=62763 {ECO:0000313|EMBL:RSD32488.1, ECO:0000313|Proteomes:UP000269041};
RN   [1] {ECO:0000313|EMBL:RSD32488.1, ECO:0000313|Proteomes:UP000269041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 594 {ECO:0000313|EMBL:RSD32488.1,
RC   ECO:0000313|Proteomes:UP000269041};
RA   Gomez-Gil B., Enciso-Ibarra K.;
RT   "Genomic taxonomy of the Vibrionaceae family.";
RL   Submitted (DEC-2018) 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   -!- 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:RSD32488.1}.
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DR   EMBL; RSFA01000008; RSD32488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R9FP12; -.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000269041; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR033414; Sensor_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF17149; CHASE5; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW   Kinase {ECO:0000313|EMBL:RSD32488.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Transferase {ECO:0000313|EMBL:RSD32488.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          254..475
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          624..744
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          779..899
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          220..247
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         673
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         829
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   900 AA;  102041 MW;  5DAED2D5C4738D2C CRC64;
     MKNKRRYLSI NKKLLFAVTL ISIFLALTTT SYNLYYRLQL DIDHITKTLS NIKNSQLSSI
     TGSLWVEDRV LLESQIEGLL TLPGVDYANI WNDRESVIEK GERLSEGAIT QIWPLEYQLG
     GKNYVLGNLI IQSDLTRTYA SLWSQFVHIL SAESVRIMLL LTSVLFFTWF FVIKRINLME
     KIVSSSKNNQ SLNKIFLPSS WFNDEITHLA DKFNQSGDII EAHYSQLNQA REDAERAKDE
     AIRASKAKSS FLANMSHEIR TPLNGVIGIS EVLSDTSLTA TQRDYVDTIE TSSHLLLNLI
     NDILDFSKIE SGMLVISPNS TNVRESIYDI VSIVSPRAQE KEIDLRVTVS SGLPYCLMID
     DHRLRQVIMN FMSNAVKFTE KGSVHLSIIT RDVTAENAIV EFSVHDSGIG IDEQQQNKIF
     EPFKQEDDST TRQFGGTGLG LAISTQLVEL MGGKIQLESE KNQGSRFFFQ LSLPIAQMDY
     NSKHTSRLSP LCLVCDDKVM EEQLCESLNF YHAPVYQSIT SLDYLPKWVH EKDNVIVIYV
     ETSPNTAVKR ESLFRHLKAL NIHVCLMKHL RSQQYDFGEN VSAIITQPLL GQRLVKVIER
     LEQDLEQSST QELQRIRDDI ITKKILVVDD NEVNRKIATI HVEKAGFSFD LAENGQQAVE
     MFKKHHYALI LMDCMMPVMD GFEATEKIRQ IEHEENRAKR IPIIALTASV VDEDIQKCFK
     VGMDDYVAKP FKAEVLRGKL TIFVSQDSVE TLSLPTASES QKVSVNLEPN DTVSNCIGRI
     LLVEDNNVNQ KVASLMLSKA GYQFEIAENG QVALDKYEQD SSFDIILMDC MMPVMDGFEA
     TQKIREYEHC LGLAKTPIIA LTASVVDDDI RRCFDSGMDA YLPKPFRKET LLNEIESITS
//
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