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PBPA_CLOB1
ID   PBPA_CLOB1              Reviewed;         830 AA.
AC   A7FY32;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Penicillin-binding protein 1A;
DE            Short=PBP1a;
DE   Includes:
DE     RecName: Full=Penicillin-insensitive transglycosylase;
DE              EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
DE     AltName: Full=Peptidoglycan TGase;
DE   Includes:
DE     RecName: Full=Penicillin-sensitive transpeptidase;
DE              EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
DE     AltName: Full=DD-transpeptidase;
GN   Name=pbpA; OrderedLocusNames=CLB_3112;
OS   Clostridium botulinum (strain ATCC 19397 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19397 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC       from the lipid intermediates. The enzyme has a penicillin-insensitive
CC       transglycosylase N-terminal domain (formation of linear glycan strands)
CC       and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC       linking of the peptide subunits). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000250|UniProtKB:P02918};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000250|UniProtKB:P02918};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000305}.
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DR   EMBL; CP000726; ABS35652.1; -; Genomic_DNA.
DR   RefSeq; WP_012048098.1; NC_009697.1.
DR   AlphaFoldDB; A7FY32; -.
DR   SMR; A7FY32; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   GeneID; 5185759; -.
DR   KEGG; cba:CLB_3112; -.
DR   HOGENOM; CLU_006354_2_2_9; -.
DR   OMA; AVQMPYI; -.
DR   OrthoDB; 652304at2; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; -; 1.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Carboxypeptidase; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Hydrolase; Membrane;
KW   Multifunctional enzyme; Peptidoglycan synthesis; Protease; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..830
FT                   /note="Penicillin-binding protein 1A"
FT                   /id="PRO_0000321873"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..830
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          57..229
FT                   /note="Transglycosylase"
FT                   /evidence="ECO:0000250"
FT   REGION          357..641
FT                   /note="Transpeptidase"
FT                   /evidence="ECO:0000250"
FT   REGION          754..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..786
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..817
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        96
FT                   /note="Proton donor; for transglycosylase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P02919"
FT   ACT_SITE        398
FT                   /note="Acyl-ester intermediate; for transpeptidase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P02919"
SQ   SEQUENCE   830 AA;  92704 MW;  DF9752C616B6D2C1 CRC64;
     MGKKKKKRKS SAFKIILNVF LSIFLVAGVA FGGIVFAMIK TAPPLNVQQV LTFDEPSILY
     DDKGQYMDKV ITNEQRIVVD YKNVPQNLKN AFVSIEDERF YKHHGVDIKR FTGVILINVT
     NKIKRSSKLQ GASTLTQQLI KNTVLSSEVS IKRKVQEMYL SIQLEKELSK DEILGAYMNS
     IFLGGNALGV EAASKQYFNK SVKDLSLIEC AFIAGVPQSP SVYYPYSSAS KKNPSIYLNR
     TKTVLYKMLD NGYITQNDYN KALKDLDSKK LVFAKPSAPS NKLAYEWFSI PAIEQVKKDL
     KTQYKYDDKQ IHNLLVNGGL KVYTTMNKNL QDKTQNTINN AYYLNSYKSN GMIYPQASAV
     IMDYHNGEVK TIIGGRGDQP ARSYNRAASY NYLRPAGSSI KPLTVYSAAI DSKKATAATG
     FEDSPIPNNI GRKYSSGAPY NPKNSPDIYY GYVNVREALM RSINVVAVKL VDKIGLNTSI
     QYAEKFGIPI DQHDRSSIAS LSLGELHKGT NPLIMAQAYG VFGNNGTYTE AKLYTKVVDR
     TGKVLLEPKT NTKKVLSPEA AFITYDMLQG PVSESGTGPQ ANFGNMEVRG KTGTSSDMKN
     LWFCGLTPYY SAAVWIGNDN SSTVDGVYSS TAARLWGDIM KEFHVNLPYK QVQKPASVVT
     ANVDRISGKL PTQLSYRDPR GSTVYNEFFI NGTIPTEYDD IHVEAQINKL TGKLASKFTP
     SFLVESRVFL RRDYSPGVEL LDQQWLLPYS IDEGGSLPPT EEKNNSNTRD KNKDKNKNKN
     KDKNPSQDKP NNNNNDNNSN NNNNNNDNNN NTKPPENDSN QNHEDNKNKQ
 
 
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