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
//