ID Q1ZSC7_PHOAS Unreviewed; 971 AA.
AC Q1ZSC7;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Phosphorelay protein LuxU {ECO:0000256|ARBA:ARBA00017260};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VAS14_05003 {ECO:0000313|EMBL:EAS65050.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS65050.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS65050.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS65050.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:EAS65050.1}.
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DR EMBL; AAOJ01000002; EAS65050.1; -; Genomic_DNA.
DR RefSeq; WP_005368617.1; NZ_CH902600.1.
DR AlphaFoldDB; Q1ZSC7; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG4192; Bacteria.
DR HOGENOM; CLU_000445_40_1_6; -.
DR OrthoDB; 6724607at2; -.
DR Proteomes; UP000001603; 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; cd06225; HAMP; 1.
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 CDD; cd16172; TorS_sensor_domain; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.58.920; -; 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 Gene3D; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR037952; Sensor_TorS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR014302; Sig_transdc_His_kinase_TorS.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR038188; TorS_sensor_sf.
DR NCBIfam; TIGR02956; TMAO_torS; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 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; PF21689; TorS_sensor_domain; 1.
DR PIRSF; PIRSF036437; HK_TorS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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: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};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 365..412
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 476..694
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 712..834
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 876..971
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 413..466
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 761
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 915
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 971 AA; 107557 MW; 209C1BDFF035DCA2 CRC64;
MTSTLKGIGT KLLIAFSAMA SLMIIAVMIG VAGFSLVAKT ERTVINSAVP ALAEARQLSD
LSSRIIFNAQ VLAKSKAESE RMRQGRALTV HIEALNRSLH SLEQFSFDQP LMVKLEEDVK
RIVDNLALLG LLVGRQIDLQ SQLDKLTTEM TKATHQIDNL SQSQVSNAST IAVANVSRIY
DLVADGNKPA VYKALDSLVE VDMDLSERLF ELRFLSLQVI NMLDDSSRIA DIKSLVALKK
RYNDAVGIMS QRVKSVEDPS RSEQLVELTA QLNRGRLLFG VIEQLIYAKQ DVERLDQQNL
VLFQQLNNTV DDIIDVANVN TQQAVKRVDH TLTLARNTLI VISAIGLLAL VLIMWRFVYA
RVICRINEYS RALSALTRGD LGVKINVKGD DELAQMGRAI LVARDTANER YRLAQAESKA
RQELQEHKAS LERLVAKRTG ELEKINRRLN EEVHNHYKAR DEAEKANRAK SSFLATMSHE
IRTPMNGVLG TASLLADTQL TSQQKRYLDV INRSGETLLD ILNDILDYSK IEAGHLDIRP
SNFSVVRMVT DVSSMLEGRA LAKRIGLECH ISPQVEGMWF GDESRIRQVL VNLVGNAIKF
TDTGKVSIFV EPHPDMPDEL LFSVKDTGIG IDQEEQNILF SAFQQAEAGR KSIEGTGLGL
AISKHIVAAM DGEIGLESVV GEGSCFWFAL PLEHGEGSLE PDDKRVIMRS AHILLVEDNP
INSMVAEGFL TRLGHTVVTA TDGAEAEEIY KKQRFDIALL DINLPDTDGV QLLSRLRRLE
DNNHEAWEEP TPMVAFSAHV FREEVELYLN AGFAGFLPKP LVEKQLIDTM SSILKGEKRV
IIEKGIGEES VEVKQTENTI PLLKESVLGS DLQVLGEAQV KQLIHLFGES SSLTLSKLHQ
AIDDENLSEV AKQAHTLKGA AGTMGLMQLH HICSEFEKNA KEGSINSLDL SSLQRVFDQS
VGILKTTFIS A
//
