ID B5XXR0_KLEP3 Unreviewed; 833 AA.
AC B5XXR0;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Multiphosphoryl transfer protein 2 {ECO:0000313|EMBL:ACI11868.1};
DE EC=2.7.3.9 {ECO:0000313|EMBL:ACI11868.1};
GN Name=ptsA {ECO:0000313|EMBL:ACI11868.1};
GN OrderedLocusNames=KPK_3550 {ECO:0000313|EMBL:ACI11868.1};
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI11868.1, ECO:0000313|Proteomes:UP000001734};
RN [1] {ECO:0000313|EMBL:ACI11868.1, ECO:0000313|Proteomes:UP000001734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:ACI11868.1,
RC ECO:0000313|Proteomes:UP000001734};
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC fructose 1-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:49252, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:37721, ChEBI:CHEBI:58674,
CC ChEBI:CHEBI:64837; EC=2.7.1.202;
CC Evidence={ECO:0000256|ARBA:ARBA00001401};
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}.
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DR EMBL; CP000964; ACI11868.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XXR0; -.
DR KEGG; kpe:KPK_3550; -.
DR HOGENOM; CLU_007308_5_0_6; -.
DR Proteomes; UP000001734; Chromosome.
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:SF4; MULTIPHOSPHORYL TRANSFER PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46244; 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; 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; 1.
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; 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 Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACI11868.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 2..91
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
FT DOMAIN 688..830
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
SQ SEQUENCE 833 AA; 91801 MW; B5B14E9C2082A4CB CRC64;
MALVIEFTCD LPNGVHARPA SLVETLCNRF SSAIEWRNLR RETGGNAKSA LAIIGSNTLK
GDACQLLISG EDEAEAFAAL TAFMRDEFPH CDAPLPAAPT LDVQPVPESL SRLNPTLFHA
HPVCAGSAGG ALVHLKSRDL HELGELPVAA SPEQEQAALD NGLRLLVKDI ELRLLDNDGT
ASAILEAHRS LATDASLRQH LLGGILTGLS CAQAIVATGD HFCAQFRDSG NSYLQERVLD
VRDVCFQLLQ HIYGEARFPA PGQLREAAIC LADELTPSQF LELDKTHLKG LLLRSGGTTS
HTVILARSFN IPTLVGVDLA ALLPWVDTQV QIDGNAGLLV VDPSPAVARY YQQEAWLQAQ
IRQQQQVWLD KAGQTQDGIR VEIAANIAHS VEAVAAFNQG AQSVGLFRTE MLYMDRPSAP
SEDELYNIFC QALEPAAGRS IIVRTMDIGG DKPVAYLNIP AENNPFLGYR AVRIYEEYQA
LFHTQLRAIL RASAHGSLKI MIPMISSMEE ILWVKERLAE AKQSLRAEQI PFDEKIPLGI
MLEVPSVMFI IDQCCEEVDF FSIGSNDLTQ YLLAVDRDNA KVTRHYNSLN PAFLRALDYA
VQAVHRQGKW IGLCGELGAK GSVLPLLVGL GLDELSMSAP AIPATKSRLA QLDSRACRQL
LNQAMQCRTS LEVEHLLAQF RMRQQDVPLV SAECITLNSD WRSKEEVLKG MTDNLLLAGR
CRYPRKLEAD LWAREAVFST GLGFSFAIPH SKSEHIEQST ISVARLAQPV IWGDEEAQFV
IMLTLNKHSA GDQHMRIFSR LARRIMHAEF RQSLVSAESS EDIADLLRRE LEL
//
