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Database: UniProt
Entry: A0A2G8E378_9GAMM
LinkDB: A0A2G8E378_9GAMM
Original site: A0A2G8E378_9GAMM 
ID   A0A2G8E378_9GAMM        Unreviewed;       377 AA.
AC   A0A2G8E378;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Multiphosphoryl transfer protein {ECO:0000256|ARBA:ARBA00015565};
GN   ORFNames=BK416_15575 {ECO:0000313|EMBL:PIJ68974.1};
OS   Erwinia sp. OLSSP12.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1912096 {ECO:0000313|EMBL:PIJ68974.1, ECO:0000313|Proteomes:UP000229786};
RN   [1] {ECO:0000313|EMBL:PIJ68974.1, ECO:0000313|Proteomes:UP000229786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLSSP12 {ECO:0000313|EMBL:PIJ68974.1,
RC   ECO:0000313|Proteomes:UP000229786};
RX   PubMed=29067021; DOI=10.3389/fmicb.2017.01969;
RA   Chen X., Hitchings M.D., Mendoza J.E., Balanza V., Facey P.D., Dyson P.J.,
RA   Bielza P., Del Sol R.;
RT   "Comparative Genomics of Facultative Bacterial Symbionts Isolated from
RT   European Orius Species Reveals an Ancestral Symbiotic Association.";
RL   Front. Microbiol. 8:1969-1969(2017).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. The
CC       enzyme II FruAB PTS system is involved in fructose transport.
CC       {ECO:0000256|ARBA:ARBA00003136}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:PIJ68974.1}.
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DR   EMBL; MNCH01000045; PIJ68974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8E378; -.
DR   OrthoDB; 1640042at2; -.
DR   Proteomes; UP000229786; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd00367; PTS-HPr_like; 1.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   Gene3D; 3.30.1340.10; HPr-like; 1.
DR   InterPro; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_sf.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR001020; PTS_HPr_His_P_site.
DR   InterPro; IPR002114; PTS_HPr_Ser_P_site.
DR   NCBIfam; TIGR01003; PTS_HPr_family; 1.
DR   PANTHER; PTHR30181; MANNITOL PERMEASE IIC COMPONENT; 1.
DR   PANTHER; PTHR30181:SF3; MULTIPHOSPHORYL TRANSFER PROTEIN; 1.
DR   Pfam; PF00381; PTS-HPr; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   PRINTS; PR00107; PHOSPHOCPHPR.
DR   SUPFAM; SSF55594; HPr-like; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 2.
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.
DR   PROSITE; PS00589; PTS_HPR_SER; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000229786};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022597}.
FT   DOMAIN          2..142
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
FT   DOMAIN          285..375
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
SQ   SEQUENCE   377 AA;  39843 MW;  C5212E26D995AAC7 CRC64;
     MFQLDLSAVH IGAAASNKEQ AIRQVAAALI DAGNVTEGYS EGMLAREQQT STYLGNGIAI
     PHGTTDTREQ VLNTGVQVFQ FPQGIDWGSE QQAFIVIGIA AKSDEHLTLL RQLTHVLSDE
     SVAQQLRETD SADRLRSLLM GEHQPAELHF DPAMIATEVA ADDFITLQAL NAGRLQKAGA
     VNADFIRHAL ASTPLNLGQG IWLSDSPLGN LRSAVAISRS ATPFEVDGES AALLITVAVT
     DDQPLTVLNH LSDLLIARQG EQLLRADAAG IIALLTGSTN QTDDTLTADF TIRNEHGLHA
     RPGTVLVSVI KQFSSDITIT NLDGSGKPAN GRSLMKVVAL GVKKGHRLRF SASGADAAQA
     LQAIEEAINS GLGEGAV
//
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