ID U4KE59_9VIBR Unreviewed; 892 AA.
AC U4KE59;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VIBNI_A1036 {ECO:0000313|EMBL:CCO57188.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO57188.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO57188.1, 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO203526; CCO57188.1; -; Genomic_DNA.
DR RefSeq; WP_022550189.1; NC_022528.1.
DR AlphaFoldDB; U4KE59; -.
DR STRING; 28173.VIBNI_A1036; -.
DR KEGG; vni:VIBNI_A1036; -.
DR PATRIC; fig|1260221.3.peg.999; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000016895; Chromosome 1.
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; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
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; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; 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; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCO57188.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 306..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 330..382
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 443..662
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 686..801
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 384..443
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 735
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 892 AA; 100175 MW; 5193EE5DCB32400C CRC64;
MTFKTKLFVF TPLLVALTIV LSIVASNVLM RSEINRQNEA RLHNATSSLQ RRILDDFPHI
HRQYEAFRNS GSTQFLMGVE RGSVFTAEDF LGVLTFYPDV REYLLEFARL YDITSYAIYL
PADPNSKAPV FDEGVNYLYA QYNAELDGII LNESTLISWD ARNFLRKKEI TPVLNFPKKF
VGSAGTELAT LSDGSIGISY SFELDNGGIL VLQRSWDFDL AIQEVDLGVE ITLYDEDRQR
IDGSKLFRVL TDEVPVGTPK KLMELQDVDG QIHTGLASTI RDKGVILGYL VTSISQQVIE
DATKRVAVLL ILSGLVLVLL AVAIAILMAR SFIEPISQLI KDFSAIANGN INHKINISRR
DEFGELARNF YFMQSAIKDN ITELNLKIQE RDVAERKVRK LNEELEDRVM QRTEELRHAV
GEMEKAKEGA EKANQAKSEF LANMSHEIRT PMNAILGFSE ILHSEETNPK KLNFINKIRT
SGKALLHLIN DVLDLSKVEA GKLEFHMAAT SVPKMFEELH DMFEHKATSS NLALIYEIEK
GMPESLLLDE NRLRQVFINL IGNAVKFTEQ GYVKVTSRAI PVDNDFRLEF DVEDTGIGIR
EDQIGKIFGS FEQAEATESR FGGTGLGLAI SRQIIELMGG QISVKSEFGV GTTFSVTLPI
VKSAQEIEQD SGEHSPNQKV AFEPAKILIA DDVDYNQEIL AQFLSDSPFS LDYADDGLQV
LERVERFVPD LILMDIKMPN MDGREASEKL KNDPRFKDIP IIAVTASALS DSLDTYIQHC
EGYITKPVDK DSLTEELKKF LAYTRVNGVA NSAVALQSQP AEVEGEIRVP GGEILTKIRA
LAIDGYIDDI QELMQPLSTD FPEFTERVVK FAHEFDDQKI IDMVDDYVNE QP
//
