ID K0YMT6_9ACTO Unreviewed; 574 AA.
AC K0YMT6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000313|EMBL:EJZ84967.1};
GN ORFNames=HMPREF9240_01864 {ECO:0000313|EMBL:EJZ84967.1};
OS Winkia neuii BV029A5.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Winkia.
OX NCBI_TaxID=888439 {ECO:0000313|EMBL:EJZ84967.1, ECO:0000313|Proteomes:UP000006075};
RN [1] {ECO:0000313|EMBL:EJZ84967.1, ECO:0000313|Proteomes:UP000006075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BVS029A5 {ECO:0000313|EMBL:EJZ84967.1,
RC ECO:0000313|Proteomes:UP000006075};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinomyces neuii subsp. anitratus BVS029A5.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EJZ84967.1}.
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DR EMBL; AGWP01000010; EJZ84967.1; -; Genomic_DNA.
DR RefSeq; WP_004808341.1; NZ_JH815218.1.
DR AlphaFoldDB; K0YMT6; -.
DR PATRIC; fig|888439.3.peg.1872; -.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_7_0_11; -.
DR Proteomes; UP000006075; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
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; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
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 PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 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 SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyruvate {ECO:0000313|EMBL:EJZ84967.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006075};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJZ84967.1}.
FT DOMAIN 8..126
FT /note="Phosphotransferase system enzyme I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05524"
FT DOMAIN 152..224
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 248..524
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 574 AA; 61433 MW; B343971E430401ED CRC64;
MDARINARGI PVVTGAAFAP VRWVVRPQPI SLDSQTVPKE LRDHEVERFV EAADNVTARL
LSRAEKSVGS SSDLLRVAAA MATDPAWRSA TTKLIQAGTP ADSAATQTIA DIARKFVAAG
DTLAERVTDL IDVRDRVVAE IHGMPEGALP ELDKPTILFC DDLAPADAGA LDPKYVKALV
CRGGGPTSHF VIVSRQLGIP CIISAKGIDN VEDGELALVD GANGHITINP DAGHARSIIA
LDEARHQAED NWEGPACTKD GIRIYLYGNV QDRMQALQAR KMGADGVGLL RTELTFLGTR
NEPNLDAQIR AYKSVIDVFP DKRFIARTLD AGSDKPVVWA GTQPEENPAL GVRGLRTILR
KKEVLLHQLD ALAEVSAGRK EPLRVMAPMV STLDEAQMFA DLVRERGMSP GIMIEVPALA
FLADPLYQIV DFTSLGTNDL TQYLMAADRT NPYLASYLDA WQPAILTLIA HVARAAARHG
KQACVCGEAA ADPVLASVLT GMGVHGLSMA PSAIKTVGSY ISQLNLDTCK RAAIAVIGND
PGDMYGPYTG AFSAVDARER ALKIFNEALS ATQN
//
