ID N9MR13_9GAMM Unreviewed; 954 AA.
AC N9MR13;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=F897_00698 {ECO:0000313|EMBL:ENX11014.1};
OS Acinetobacter variabilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=70346 {ECO:0000313|EMBL:ENX11014.1, ECO:0000313|Proteomes:UP000013101};
RN [1] {ECO:0000313|EMBL:ENX11014.1, ECO:0000313|Proteomes:UP000013101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 2171 {ECO:0000313|EMBL:ENX11014.1,
RC ECO:0000313|Proteomes:UP000013101};
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 sp. NIPH 2171.";
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:ENX11014.1}.
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DR EMBL; APRS01000005; ENX11014.1; -; Genomic_DNA.
DR RefSeq; WP_005233291.1; NZ_KB850112.1.
DR AlphaFoldDB; N9MR13; -.
DR STRING; 70346.F897_00698; -.
DR GeneID; 75330279; -.
DR PATRIC; fig|1217693.3.peg.677; -.
DR HOGENOM; CLU_007308_2_1_6; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000013101; 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 CDD; cd00367; PTS-HPr_like; 1.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR Gene3D; 3.30.1340.10; HPr-like; 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; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_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; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
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; 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 Pfam; PF00381; PTS-HPr; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55594; HPr-like; 1.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 2.
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.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 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:ENX11014.1};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ENX11014.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
SQ SEQUENCE 954 AA; 103638 MW; 69E9D77449BEDEB9 CRC64;
MLALDIQHVR MKQHATDKAQ ALQCLVDILV EDQLVTPDYI HGLTVREQQS ATYLGQGIAI
PHGTPQSRQC ILKTGIRLAH FPEGVVWDGE NKIYLAVVIA AKSDEHLQVL QILTRALIND
VADQVKQAQS AEQIIALLQA QPASLALHEN LIATQVPALD VEDLIWQATQ LLKQQKMVEC
GFLSGLNLNS MIHLGEGVWS ITSNQHVLSP AVSLVKAEQV LSHQQEMLKT LVCIASNEQL
DMQRFQRLMD ILFDTEQVHT LNQEQDSHQL AQLIGAELIP DWPSRRIVLA NAHGLHARPA
THLVNMTKKF AGDILVAVDE GAYVSAKSLT KLLAMGCRRG QTLTFIAQPD TDAVAGLEQI
IDAVQQGLGE EVEAVDLVSH QHSSSAPVVN NLELMPFESH GDTGSCGIAA STGLAFGPAH
VVKPHEFSYE RRGQSFKAEN EKLEIALHQV KNNLRQFIAH TESTAIKQIF MAHLEMLDDP
DLLQSVQRGL KQGLSAAAAW HDHIEVAATA QAALSDRLLA ERAADLRDIG ERVLAALCGV
ADVTEPEQPY ILIMHDVGPS DVARLNKDRV AGILTAVGGA SAHSAIVARA LAIPAVVGAG
VAVLNIENHA TVLINGDSGE YVVSPEQNQI DHAIAERQRQ RELREQAEQH CLEPAITLDQ
HQVEIAANIG KVGATIQAVA DGAEAIGLLR TELVFMSHSS APDEATQEAD YRVVLDALAD
RPLVVRTLDV GGDKPLPYLP IEKEENPFLG LRGIRLTLRK PELLRQQLVA LLKAADNRPL
RIMFPMIGRV EEWRAAKAIL DEVRIQHPCE NLQVGIMIEV PAAALLAPIL AQEVDFFSIG
TNDLTQYTLA IDRGHPLLSA EADGLHPSIL LLIDQTVRAA HQHGKWVGIC GELAADPKAV
PVLIGLGVDE LSMSSTSIPL VKAQIRGLNY INCQQVAQQA LSCDSATAVR ALVE
//
