ID Q7MFJ1_VIBVY Unreviewed; 1243 AA.
AC Q7MFJ1;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Phosphorelay protein LuxU {ECO:0000256|ARBA:ARBA00017260};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=VVA0329 {ECO:0000313|EMBL:BAC96355.1};
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC96355.1, ECO:0000313|Proteomes:UP000002675};
RN [1] {ECO:0000313|EMBL:BAC96355.1, ECO:0000313|Proteomes:UP000002675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016 {ECO:0000313|EMBL:BAC96355.1,
RC ECO:0000313|Proteomes:UP000002675};
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA Tsai S.F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}.
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DR EMBL; BA000038; BAC96355.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7MFJ1; -.
DR STRING; 672.VV93_v1c33130; -.
DR KEGG; vvy:VVA0329; -.
DR PATRIC; fig|196600.6.peg.3535; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_37_4_6; -.
DR Proteomes; UP000002675; Chromosome II.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd00088; HPT; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 2.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000313|EMBL:BAC96355.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:BAC96355.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 527..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 706..922
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1021..1138
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1140..1242
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 549..583
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1071
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1188
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1243 AA; 140344 MW; 134CB607A46CE05A CRC64;
MNLLKSQNLT NSHIILILYS IFEEYKMLNA HIRFVSFLIL LSGLLFSGNA LPQEENSEQE
TNPPSTIVIG ITSKSINPSL DSESLGVYWG VNVEYLRNIA KILNINIQLK HYSNVVELLH
DVETGTIDGT VGFAKTPERM NRFLFSKPLF KSSVSIWFKE SFYQTRPFST LNWTCVKGTS
YCEYLRIKGI KNIHYALNFT DAVAIMNKGQ ANAFISSFVT INEYLDKHDV VRGAVEIPDW
IEPEEISFIT AKNNVALMES IDKVLEWEVK GKNIRSVASN NLYHLNDRLL SEYRREHHDD
DVITFSTSNN AYPFFEISDN GEPRGLLADF LDLIQSRSGL DFEYKSPIFE YNQELATFNA
NIIPVAYIDR VESPNWLLTK PFMQIKFHKV ELASAKAINN RKPISGILLS LQKQGLIHIN
AWNNENFREY SDIKKLMKDL EDGKIQSAYL SDDVLYSLLS QFNKGQLKID KSQEKRFSIA
FSVSNHDIKL KKLLDSIIDT IDSKEIEKIN KSYRDFNLTY GYDSETVIFS AIVISVVLII
IAIIIYFVIT NMKLKVSLAE INADNEEKEK QWLTQIIQEL NNKVFIHDDK GQLVLSNCSE
YLKGNCTNCQ IKNAATQISL VGDFEEVQQV LRGKRIKEYS QTVNCDLQIE HIYRERKAIR
SLDHRKQFVL TVLQDVTAQK EREAALIAAQ HEAQSAVKAR ERFLATMSHE LRTPLAATYG
LLDLVATHST SERDKELVLR AKQSLNHLNL LVDEVLDYSK LEAGELQIHP AKNELLRLLS
QTLRGFEAKA NSKGLDYTVN IIPFSLRWAM IDDLRFNQIV SNLISNAIKF TEQGDITLTA
QVVKERLLLT IKDTGIGMTQ EQLANIFKPF VQADDSITRQ FGGTGLGLAI VEQLLKQMGG
HIALHSALNV GTQVDIELPL TPCEGAYPEL NALSYSSQLP TVIQDWCQCW GLVKNDANPS
VNKGLSGECN TLSCQPSGCQ RNSALECTQY PDALLDCLLK MTSTEQERHI EEIPMDALAG
KVLVAEDNKI NQHIVKMQFA ELGLTPIVVN NGLEALNYIK QHGDVALLLT DFHMPEMDGY
ELVKTLRANE RFAALPVVGV TAEDSRIANE KSMQSGINEI LYKPYDLKQL GALLARYLAK
PKARENWLDK FSENDAQEVA KVFIVEMAKD LTQLKQAESG HQMRAAVHKV KGACGALGIQ
HIVALCQDAE SVDMAHKPAL VEKVISELDA EINRTIMWME SYA
//
