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}.
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; 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
//