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Entry: A0A1E7R313_9GAMM
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ID   A0A1E7R313_9GAMM        Unreviewed;       765 AA.
AC   A0A1E7R313;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   Name=ptsP {ECO:0000313|EMBL:KAA8733835.1};
GN   ORFNames=BJI46_04205 {ECO:0000313|EMBL:OEY93653.1}, F4V57_07230
GN   {ECO:0000313|EMBL:KAA8733835.1};
OS   Acinetobacter qingfengensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1262585 {ECO:0000313|EMBL:OEY93653.1, ECO:0000313|Proteomes:UP000185895};
RN   [1] {ECO:0000313|EMBL:OEY93653.1, ECO:0000313|Proteomes:UP000185895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 4671 {ECO:0000313|EMBL:OEY93653.1,
RC   ECO:0000313|Proteomes:UP000185895};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAA8733835.1, ECO:0000313|Proteomes:UP000323633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 69710T {ECO:0000313|EMBL:KAA8733835.1,
RC   ECO:0000313|Proteomes:UP000323633};
RA   Pineiro-Iglesias B., Tunovic T., Unosson C., Inganas E., Ohlen M.,
RA   Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA   Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT   "Draft genome sequence of various Type strains from the CCUG.";
RL   Submitted (SEP-2019) 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:OEY93653.1}.
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DR   EMBL; VXKN01000004; KAA8733835.1; -; Genomic_DNA.
DR   EMBL; MKKK01000045; OEY93653.1; -; Genomic_DNA.
DR   RefSeq; WP_070070468.1; NZ_VXKN01000004.1.
DR   AlphaFoldDB; A0A1E7R313; -.
DR   STRING; 1262585.BJI46_04205; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000185895; Unassembled WGS sequence.
DR   Proteomes; UP000323633; 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   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:OEY93653.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185895};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OEY93653.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          22..169
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   765 AA;  85443 MW;  B9C4B6DA598B5A51 CRC64;
     MANTMQLETL RRIVQEVDAS PSLHEALDVM VDQVAQAMNV EVCSIYLLDE RNHRYILMAS
     HGLRPESVGN VSLDISEGLV GLVGQREEIV NLENASKHER FIYLPETGEE IYNSFLGVPV
     MYRRKVMGVL VIQNKESHDF SEAAESFLVT LCAQLSGAIA HAHAAGNIEI FRKSTSGPSY
     QLYQGVAGAD GIALGRAVIL YPAADLSAIP DREAEDISEE LVLLNNAVAA VRGDIKNLDA
     KMQDSLMSEE RALFSVFLRM LDDTALPAEI STMIRDGHWA QGAVRRVIEK HVNIFAQMED
     DYLRERVSDL KDLGRRILAY LQTADTSHKE ITEDTILIGE EISTAALVEM PIHNISAIVT
     TEGAANSHMV IVARALGIPT VVGVTELPIH TLDDAEIIVD AYQGRVFLHP PRRLRTRYKE
     IKKEEEQIAK DLKQYETKSA ITPDGHTLPL FVNTGLMIDV VRGVQRGAKG VGLYRSEIPF
     MLRERFPGEE EQRLIYRQQL SHFANKPVVM RTLDIGADKD LPYFSIDEEN SALGWRGIRF
     TLDHPEIFSS QIRAMLKASI GLNNLHILLP MVTSVSELEE VLYLLDRDLA AVQEEEQVKI
     NKPKIGIMIE VPSVLYQINE FAELVDFFSV GSNDLIQYLL AVDRNNPRVA SVYSHFHPAI
     IRALTRLIQE CHKFDKPVSI CGEMAGNPLT AILLMAMGFN TLSMSSSNIL RVRKAICHVP
     LSDAKRLLDE ALVIDNPLII KSMLEHYFRT HGLADMVKST RVVSV
//
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