ID N8TUQ5_ACILW Unreviewed; 765 AA.
AC N8TUQ5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=F980_00567 {ECO:0000313|EMBL:ENU63658.1};
OS Acinetobacter lwoffii NIPH 715.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217669 {ECO:0000313|EMBL:ENU63658.1, ECO:0000313|Proteomes:UP000018422};
RN [1] {ECO:0000313|EMBL:ENU63658.1, ECO:0000313|Proteomes:UP000018422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 715 {ECO:0000313|EMBL:ENU63658.1,
RC ECO:0000313|Proteomes:UP000018422};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., 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 Acinetobacter lwoffii NIPH 715.";
RL Submitted (FEB-2013) 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}.
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:ENU63658.1}.
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DR EMBL; APOT01000028; ENU63658.1; -; Genomic_DNA.
DR RefSeq; WP_004729445.1; NZ_KB849264.1.
DR AlphaFoldDB; N8TUQ5; -.
DR PATRIC; fig|1217669.3.peg.534; -.
DR HOGENOM; CLU_007308_7_1_6; -.
DR Proteomes; UP000018422; 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; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Pyruvate {ECO:0000313|EMBL:ENU63658.1};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ENU63658.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 21..168
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT COILED 213..247
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 765 AA; 85476 MW; D6FD359C10429A4D CRC64;
MSNMQLDTLR RIVQEINAST SLHESLDIMV KHVAEAMQVD VCSIYLLDER NQRYLLMASK
GLNAESVGHV SLQTGEGLVG LVGQREEIVN LDNAPKHERF LFLPETGEEI YNSFLGVPVM
YRRKVMGVLV VQNKESQDFS EAAESFLVTL CAQLSGVIAH AHAVGNIDVF RKPSNLPAYK
TFQGVSGSGG IALGRAVILY PPADLAAVPD READDISEEL ELLDNALNSV REEIQSLDDK
MQDALMAEER ALFSVFLRML DENALPAEIK AFIREGHWAQ GAVRIVIDNH VAQFSQMEDD
YLRERVADLK DLGRRILARL QEADASHREL TDESILIGEE ISTAALVELP VDKIAAIVTT
EGAMNSHMVI VARALGIPTV VGVTELPINT LDDVEMIVDA HQGRVFINPP RRLRSRYKEI
QKEEEQIAKD LRQYETKDAI TPDGVAVKLY VNTGLMIDVV RGVQRGAKGV GLYRSEIPFM
LRDRFPGEEE QRAIYRQQLS HFANKPVVMR TLDIGADKDL PYFSIEEENS ALGWRGIRFT
LDHPEIFSSQ IRAMLKASIG LNNLHILLPM VTSVSEVEEA LYLLERDHAA IQEEEQVKVN
KPKLGIMVEV PSVLHQIDEF SELVDFFSVG SNDLTQYLLA VDRNNPRVAN VYSHLHPAVL
RALTRLVQDC HRNEKPVSIC GEMAGDPLSA VLLMAMGFNT LSMSSSNILR VRKTICHVPM
SDAQELLAHV LKMDNPLMVK SWLEYYFRTH GLGDMVKSAS RMVSA
//