ID A0A1Y6IUM9_9VIBR Unreviewed; 748 AA.
AC A0A1Y6IUM9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN Name=ptsI_2 {ECO:0000313|EMBL:SMS01365.1};
GN ORFNames=VIM7927_02651 {ECO:0000313|EMBL:SMS01365.1};
OS Vibrio mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=474394 {ECO:0000313|EMBL:SMS01365.1, ECO:0000313|Proteomes:UP000196125};
RN [1] {ECO:0000313|EMBL:SMS01365.1, ECO:0000313|Proteomes:UP000196125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7927 {ECO:0000313|EMBL:SMS01365.1,
RC ECO:0000313|Proteomes:UP000196125};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FXXI01000004; SMS01365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6IUM9; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000196125; 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:SMS01365.1};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SMS01365.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..163
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 748 AA; 84194 MW; 364B342C26228B7E CRC64;
MLSQLREIVE RVSKVEDVHQ AFDVLVKETC EAMNTECCTI YLANEEKQRL ELIATQGLKF
KGNKIHIGFD EGLVGLVKRS AEPINLAEAS KHPHFKYFRQ LGEEVYQSFL GTPIIHRKKV
LGVLVVQQRS PRQFSEIEES FIVTLSAQLA VLVAHAQSQG LWSLSKQQSV VRGIGASPGV
AIGEFWWDNS QPELENVLPA STLDIKKEQE WLSRAVENAL SDFRRMRKKL DGDIHKETLA
IFDLFTHLLN DPMLRKDLKE QIQKGDRADW ALRQVVESYV ERFSGMSDVY LRERAQDLRE
LGQRMLYFLY NSEQEELTLE KPIILVVREL TASILASIPK DKLLAVVSLE GAANSHAAIL
SRALGIPAVM GVSLNFKEIN NKLAIVDGYS GFIHISPDSE VLAEYQELME EESELSEMAN
EGLSEKAVTL DGYPVEILLN AGLNTENNAA VNQGVDGVGL YRTEISFLLQ NRFPSEEEQT
QLYRQVLCTY PNKKVVMRTL DVGGDKPLPY LPIEEDNPFL GWRGIRFTLD HPDIFLIQLR
AMMRASTETN NLGILLPMIS GMKEFDDALA LIHQAFEEVS LVDERVKMPT IGVMVEVPSM
LYLLPQIANR VDFISVGTND LTQYLLAVDR NNARVADVYE SMHPSVLMAL KHISDVCHQY
QIDVCVCGEL AGDPIGALLL IGMGFRALSM NTSNVAKVKY LIRHSEIKTL EKLASQALMQ
PYGHDIYCMM QTHFEEFGFA GFIRAGKN
//
