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Database: UniProt
Entry: U4KDZ2_9VIBR
LinkDB: U4KDZ2_9VIBR
Original site: U4KDZ2_9VIBR 
ID   U4KDZ2_9VIBR            Unreviewed;       503 AA.
AC   U4KDZ2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=VIBNI_A0952 {ECO:0000313|EMBL:CCO57108.1};
OS   Vibrio nigripulchritudo.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO57108.1, ECO:0000313|Proteomes:UP000016895};
RN   [1] {ECO:0000313|EMBL:CCO57108.1, ECO:0000313|Proteomes:UP000016895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
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};
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DR   EMBL; FO203526; CCO57108.1; -; Genomic_DNA.
DR   RefSeq; WP_022550116.1; NC_022528.1.
DR   AlphaFoldDB; U4KDZ2; -.
DR   STRING; 28173.VIBNI_A0952; -.
DR   KEGG; vni:VIBNI_A0952; -.
DR   PATRIC; fig|1260221.3.peg.913; -.
DR   OrthoDB; 1931120at2; -.
DR   Proteomes; UP000016895; Chromosome 1.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 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; 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; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CCO57108.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW   Transferase {ECO:0000313|EMBL:CCO57108.1}.
FT   DOMAIN          17..89
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          92..144
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          141..196
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          287..502
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          251..278
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   503 AA;  57647 MW;  DEE96104A1E26E36 CRC64;
     MDEQSRLLLE LEHYRLEADR YRMLVEQSTD MISRHTPTSD WTYIDVNQAV ESMLGYLPEE
     IIGTAGYDLF HFEDADNLHE RADSVRYHNG MYINTYRYRH KMGHYIWMET TSRTIRNATG
     EPQEIVCVSR DVTDRVLAQQ SMQRFARVVE AASDLVIFCD YGTQKMTYFN ESAQQILGVP
     VENGSARYLS QLFEPEIARY RLQKALEEAD KNEGWYGSLP LQLPHSDLHA EIEEIIAHRD
     SHDKTEYYTL IGRNNTLKRQ AEEEAKQYQK EMAHMSRFLS VGEMATGLAH ELNQPLATIL
     NYCRGAQRRL ENDGNATEMV SRAFDMISTQ ALRAAEIIKR MRSFLRKADS HHQHFSINDA
     CTDVCQLLNH EIEDHNIDLS LQLAVDEPTL FGDKIQIEQV VLNLLRNAIE AHQCNDNPHR
     KVIIASSIVD REVQVLVSDN AGGISSADLG KLFEPFFTSK SMGLGMGLPI SRTIIESHGG
     RLWAEIDENA SSHFYLRLPC RGQ
//
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