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Database: UniProt
Entry: E8LSL8_9VIBR
LinkDB: E8LSL8_9VIBR
Original site: E8LSL8_9VIBR 
ID   E8LSL8_9VIBR            Unreviewed;       748 AA.
AC   E8LSL8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   ORFNames=VIBR0546_00874 {ECO:0000313|EMBL:EGA66284.1};
OS   Vibrio brasiliensis LMG 20546.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA66284.1, ECO:0000313|Proteomes:UP000004371};
RN   [1] {ECO:0000313|EMBL:EGA66284.1, ECO:0000313|Proteomes:UP000004371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA66284.1,
RC   ECO:0000313|Proteomes:UP000004371};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC         L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC         COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000683};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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:EGA66284.1}.
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DR   EMBL; AEVS01000047; EGA66284.1; -; Genomic_DNA.
DR   RefSeq; WP_006878814.1; NZ_AEVS01000047.1.
DR   AlphaFoldDB; E8LSL8; -.
DR   STRING; 945543.VIBR0546_00874; -.
DR   eggNOG; COG3605; Bacteria.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000004371; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR006318; PTS_EI-like.
DR   InterPro; IPR008731; PTS_EIN.
DR   InterPro; IPR036618; PtsI_HPr-bd_sf.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR01417; PTS_I_fam; 1.
DR   PANTHER; PTHR46244:SF1; PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM; 1.
DR   PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   PRINTS; PR01736; PHPHTRNFRASE.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Pyruvate {ECO:0000313|EMBL:EGA66284.1};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGA66284.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          17..163
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   748 AA;  84118 MW;  A193C284267540B7 CRC64;
     MLSQLREIVE QVSKVDEVHQ ALDILVKQTC SAMSTECCTV YLANEEMQRL ELMATQGLRF
     KGDKIHIRFS EGLVGLVKRS AEPLNIAKAS EHPNFKYFSE LGEEIYQSFL GTPIIYRKQV
     LGVLVVQQKS PRLFNEMEES FLVTLAAQLA VIIAHAQTQG HWRLEKKQQA IRGVPASSGV
     AIGDFWWDDT QPDLTNVYPA STLDVEREQE WLLLAIEEAL NDFRRMRKKL DSEINKDALA
     IFDLFTHLLN DPMLRKDLKA QIQKGDRADW ALRQVVESYS NRFARMSDVY LRERAQDIRE
     LGQRLLFFLH NTAQDHTVIE KPVILVVREL TATLLASIPK EKLLAVISLE GAANSHAAIL
     SRALGIPAVM GANLNPKAIK GKLGVVDGYS GKILISPNKQ LLREYRGLAN QERELADKVN
     QRIEEPAFTK DGQRVEVMLN AGLSADANIA INQGVDGVGL YRTEISFLLQ HRFPSEEEQT
     QQYQAVLNSY PDKRVVMRTL DVGGDKALPY LPIEEDNPFL GWRGIRFTLD HPDIFLMQIR
     AMMRASADHQ NLSILLPMVS GAQELDDAIA LIARAHQEVA ELDERISMPE IGVMIEVPSM
     IYLLPLIASK VDFVSIGTND LTQYLLAVDR NNSRVADVYE SMHPSVIMAL QHIHTTCEQL
     NLPVCICGEL AGDPIGALLM VGLGYRSLSM NTSNVAKVKY LLRHTETEEL RQLADKALMQ
     PYGHNIYTMM QSFFEDKGFA GFIRAGNK
//
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