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Database: UniProt
Entry: U4DRG3_9VIBR
LinkDB: U4DRG3_9VIBR
Original site: U4DRG3_9VIBR 
ID   U4DRG3_9VIBR            Unreviewed;      1028 AA.
AC   U4DRG3;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=VIBNIFTn2_1020043 {ECO:0000313|EMBL:CCN39240.1};
OS   Vibrio nigripulchritudo FTn2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1238441 {ECO:0000313|EMBL:CCN39240.1, ECO:0000313|Proteomes:UP000018247};
RN   [1] {ECO:0000313|EMBL:CCN39240.1, ECO:0000313|Proteomes:UP000018247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FTn2 {ECO:0000313|EMBL:CCN39240.1};
RX   PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA   Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA   Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT   "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT   identifies virulence-associated traits.";
RL   ISME J. 7:1985-1996(2013).
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:CCN39240.1}.
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DR   EMBL; CANW01000005; CCN39240.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4DRG3; -.
DR   Proteomes; UP000018247; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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; cd00156; REC; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.60.40.2380; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR036641; HPT_dom_sf.
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:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF07696; 7TMR-DISMED2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Kinase {ECO:0000313|EMBL:CCN39240.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Transferase {ECO:0000313|EMBL:CCN39240.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        279..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          420..637
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          649..756
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          777..890
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         695
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         826
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1028 AA;  114257 MW;  CB9A3DD1391F7CB3 CRC64;
     MSHFYSILLK FCCVTFVFLI SSLWSLDGFA HLKKTNIPIS EVSVLEDQNG TLNIADVLQA
     ENSQWQALAP SLENINMGYS DSTYWLKVVI DQPKNDCCIL TVAYTPLDYL DFYQLIDDAR
     LEHQQSGDRY PFSVRPFHDR NNTFRVVLNP DRPTVFYLRA QSESVLKLPL ELYSDIEFAQ
     TLGQENFFIG LFYGGLLLIA AYNAFVFFRL RDKVYAYYLF FVISAAHSAA CWDGLAFHYL
     WPNSPLWASK SIPISTGLLT FCTLLFSQEL LQTRKNLPWI NAIIELMKVA ALSLIVLTYL
     VPYSTVGKMS IFIAYGYGII GLVIGVASMH RKVEGSGLYL FAWSLLFVGV ISNTAANIGI
     LHSNMFTSHL IHVGGVVEVC LFSVALANRI KLLKQAKLDA ETRMSVERQM AQDKANTLAV
     ISHELRTPMN AVLGFVYLAK QGKGQLSTMD YLTKIEQASS NLVQLINDSL DFSKLEQKKL
     SLKSETFSLV DVVDHVASVS TPALAGKPVQ MYIQVAPDVP SHIRGDRVRL EQVIINLTNN
     AIKHTETGYV GLAISVIRQA GHEVVLAFNI SDSGSGISQQ YQDKLFKPYS QLEDHHKGTG
     LGLSISQKIV HLMGGNIECV SEVGRGSLFS FDLAFPLVSQ PANNSDGAHI LLVCEDETFG
     ESAKLTLRWL GMECDLVTAS QALEMTCNYD LILVDHALKG ISGETFIDIL RATDFSHIPV
     AMLCDIDDIE GSESQVEHLS KPIRVGDVFH LVNKVHGKEV SEPETSSFAD YALSGLKVLV
     ADDNKLNQEF ISDMLTMFGA DTDIVENGRQ ALEAMKKHNY DVLLLDLHMP EVDGIECAMT
     IRQTPELQQI PIFCTSASPG IVSQHMDVFD DCIAKPIIAS RLLKLLTPLA TQELSPHALP
     KKGQIRWLAD KSLPEIEGIN MSFLYEQCAY SETKVEGKLD AFVAMTEEFL TALKQTSESD
     YREKQRLYHD FAGTAGAIGA KDIQELALEL DLAWQNEQPD ESVAAELEEK TRALLDRIHA
     VPISSTVV
//
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