ID Q9AAZ4_CAUVC Unreviewed; 852 AA.
AC Q9AAZ4;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN OrderedLocusNames=CC_0448 {ECO:0000313|EMBL:AAK22435.1};
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650 {ECO:0000313|EMBL:AAK22435.1, ECO:0000313|Proteomes:UP000001816};
RN [1] {ECO:0000313|EMBL:AAK22435.1, ECO:0000313|Proteomes:UP000001816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15 {ECO:0000313|Proteomes:UP000001816};
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R., Ohta N., Maddock J.R., Potocka I.,
RA Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T.,
RA Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J.,
RA Craven M.B., Khouri H., Shetty J., Berry K., Utterback T., Tran K.,
RA Wolf A., Vamathevan J., Ermolaeva M., White O., Salzberg S.L., Venter J.C.,
RA Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK22435.1; -; Genomic_DNA.
DR PIR; G87304; G87304.
DR RefSeq; NP_419267.1; NC_002696.2.
DR RefSeq; WP_010918336.1; NC_002696.2.
DR AlphaFoldDB; Q9AAZ4; -.
DR SMR; Q9AAZ4; -.
DR STRING; 190650.CC_0448; -.
DR EnsemblBacteria; AAK22435; AAK22435; CC_0448.
DR KEGG; ccr:CC_0448; -.
DR PATRIC; fig|190650.5.peg.454; -.
DR eggNOG; COG1080; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_007308_3_2_5; -.
DR BioCyc; CAULO:CC0448-MONOMER; -.
DR Proteomes; UP000001816; 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 Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 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; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_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; IPR001127; PTS_EIIA_1_perm.
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; TIGR00830; PTBA; 1.
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; PF00358; PTS_EIIA_1; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55594; HPr-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_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 Reference proteome {ECO:0000313|Proteomes:UP000001816};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 24..128
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT DOMAIN 169..256
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
FT REGION 255..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 88445 MW; 023A8426FDEB367A CRC64;
MIVSNLVLTA PLQGWVSALE EAPDAVFAER MLGDGLAIDP LGSTLHAPCD GSVVSVHRAR
HAVTLRATNG AEILMHVGLE TVALNGEGFE VFVEEGQTVK AGDRLIGLDL DLLAQRARSL
ITPVVITNGE AFQIVRRDQD RQIGVGQFLM ELSPIAGASR AAASGAADQI TRQIIVPLAH
GIHARPAARI AQMAKTFASD LTLATGPRRA NARSPVGLMS LAIRHGDTIQ LLASGPDAQA
AVTALAELIE GGMGEGAPVA AKTSSTKTAP TKTEPSEPPP PAPLPRDGVL KGVPAAPGLA
IGKAVRLSTA EIVVREAGEG VAHEEAALAV ALETVRARIG KAAETGDKAR KAILAAHQAF
LDDPELYAGA HRLIAEGKSA GFAWRRAVGG YVQALQALGD RRMAERVDDL IDLERQVLRA
LSGEEETGAA LAPGSILLAD ELLPSQLMGA DPAALAGFAT ARGGPTSHVA ILAAAMGVPA
LVAVGGALSK VKDGATLILD ADAGTLRVAP DAKALEAAQT ALAQRQQRKA AAKAAAHEPA
VTRDGVRIEV FANTGSVADA QAAVANGAEG SGLLRTEFLF LDRETPPDED EQARQYQAIA
EALDGRPLII RTLDVGGDKA APYLPIPAEE NPALGLRGVR VSLWRPHLLK AQLRAILRVE
PRGQCKIMVP MVASLDELRA VRAVLEEAKR ELGITDRVQL GVMIETPAAA VTADLLAAEA
DFLSIGTNDL TQYVLAMDRG NPELAAGIDA LHPAVLRMID QTCQGAARHH RWVGVCGGLA
SDLDATPILL GLGVAELSTT ASIAPDVKAR VRALSLEACR ALAAQALEQT SPQAVRALVQ
GQTNTPLGGL NP
//
