ID G7TBQ5_XANOB Unreviewed; 825 AA.
AC G7TBQ5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Multiphosphoryl transfer protein {ECO:0000256|ARBA:ARBA00015565};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN Name=mtp {ECO:0000313|EMBL:AEQ96126.1};
GN ORFNames=XOC_1975 {ECO:0000313|EMBL:AEQ96126.1};
OS Xanthomonas oryzae pv. oryzicola (strain BLS256).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=383407 {ECO:0000313|EMBL:AEQ96126.1, ECO:0000313|Proteomes:UP000008851};
RN [1] {ECO:0000313|EMBL:AEQ96126.1, ECO:0000313|Proteomes:UP000008851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BLS256 {ECO:0000313|EMBL:AEQ96126.1,
RC ECO:0000313|Proteomes:UP000008851};
RX PubMed=21784931; DOI=10.1128/JB.05262-11;
RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA Leach J.E., White F.F., Salzberg S.L.;
RT "Two new complete genome sequences offer insight into host and tissue
RT specificity of plant pathogenic Xanthomonas spp.";
RL J. Bacteriol. 193:5450-5464(2011).
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 -!- 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; CP003057; AEQ96126.1; -; Genomic_DNA.
DR AlphaFoldDB; G7TBQ5; -.
DR KEGG; xor:XOC_1975; -.
DR eggNOG; COG1080; Bacteria.
DR eggNOG; COG1925; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_007308_4_0_6; -.
DR Proteomes; UP000008851; 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; IPR002114; PTS_HPr_Ser_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; TIGR01003; PTS_HPr_family; 1.
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; 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; PS51257; PROKAR_LIPOPROTEIN; 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.
DR PROSITE; PS00589; PTS_HPR_SER; 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};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..134
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
FT DOMAIN 148..240
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
SQ SEQUENCE 825 AA; 86976 MW; 71BEB3ED241F0328 CRC64;
MRLRASARDK DDAIAQAAQL LVAAGCVAPG YDASMRHREG LANTFLGHGL AIPHGVGEDR
HLVLRDGIAV LQLPEGVEWN PGQTTRLVVG IAAQSDTHIT LLRRLTRLIQ DPAQLEALFS
TNDPGVIVAA LTGDRAPDTS AAPATDLAET FEWTIAYPSG LHARPATRWA ETARGFSARA
QVRAGDQAAD AKSLVGLLQL GLRAGDSITV SAEGSDAAAL LKRLRAVMDS LTAQEKADAE
RAAQRRAAPV AGWTPPQAQP AIVGIGASPG VAIGIVHRLR AAQTQVADQP VGLGDGGAQL
HDALTRTRQQ LAAIQDDTQR RLGASDAAIF KAQAELLNDT DLITRTCQLM VEGHGVAWSW
HQAVEQTASG LAALGNPVLA GRAADLRDVG RRVLTQLDPA AASAGLTDLP AQPCILLASD
LSPSDTANLD TARVLGLATA QGGPTSHTAI LSRTLGLPAL VAAGGQLLDI EDGVTAIIDG
SSGRLYLNPS ELDLDAARTH IAEQQVIRER EAAQRALPAE TTDGHHIDIG ANVNLPDQVA
MALTQGAEGV GLMRTEFLFL ESGRTPSEDE QHATYLAMAQ ALDGRPLIVR ALDIGGDKQV
AHLELPHEEN PFLGVRGARL LLRRPDLLEP QLRALYRAAK DGARLSIMFP MITSVPELIA
LRAICARIRA ELDAPEVPIG IMIEVPAAAA QADVLARHAD FFSIGTNDLT QYVLAIDRQN
PELAAEADSL HPAVLRMIRS TIEGARTHGR WVGVCGGLAG DAFGASLLAG LGVQELSMTP
NDIPAVKARL RGTALRQLQE LAEQALACET AEQVRALEAK REDAA
//
