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PBPB_BUCAI
ID   PBPB_BUCAI              Reviewed;         760 AA.
AC   P57296;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Penicillin-binding protein 1B;
DE            Short=PBP-1b;
DE            Short=PBP1b;
DE   AltName: Full=Murein polymerase;
DE   Includes:
DE     RecName: Full=Penicillin-insensitive transglycosylase;
DE              EC=2.4.1.129 {ECO:0000250|UniProtKB:P02919};
DE     AltName: Full=Peptidoglycan TGase;
DE     AltName: Full=Peptidoglycan glycosyltransferase;
DE   Includes:
DE     RecName: Full=Penicillin-sensitive transpeptidase;
DE              EC=3.4.16.4 {ECO:0000250|UniProtKB:P02919};
DE     AltName: Full=DD-transpeptidase;
GN   Name=mrcB; OrderedLocusNames=BU200;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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) (By similarity). {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:P02919};
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:P02919};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
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; BA000003; BAB12917.1; -; Genomic_DNA.
DR   RefSeq; NP_240031.1; NC_002528.1.
DR   RefSeq; WP_010895998.1; NC_002528.1.
DR   AlphaFoldDB; P57296; -.
DR   SMR; P57296; -.
DR   STRING; 107806.10038882; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   EnsemblBacteria; BAB12917; BAB12917; BAB12917.
DR   KEGG; buc:BU200; -.
DR   PATRIC; fig|107806.10.peg.211; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_7_6; -.
DR   OMA; VHGMGLA; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
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; IPR011813; PBP_1b.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR028166; UB2H.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   Pfam; PF14814; UB2H; 1.
DR   PIRSF; PIRSF002799; PBP_1b; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR02071; PBP_1b; 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;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..760
FT                   /note="Penicillin-binding protein 1B"
FT                   /id="PRO_0000083185"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..760
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          136..308
FT                   /note="Transglycosylase"
FT   REGION          392..684
FT                   /note="Transpeptidase"
FT   ACT_SITE        174
FT                   /note="Proton donor; for transglycosylase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P02919"
FT   ACT_SITE        451
FT                   /note="Acyl-ester intermediate; for transpeptidase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P02919"
SQ   SEQUENCE   760 AA;  88003 MW;  00B2C5B51F6947D3 CRC64;
     MFFNFKKYFL IKVFFFVLIL TLCYGLYLYV KINRFINGKV WNFPTSIYGR IVNLEPGNSY
     SQKEVLHLLK STMYRKVDLV MLPGEYSIKN NTIEFIRRAF DFPDIREDEF HARLYFNKDT
     LVKIKNIDNN HDFSFFRLEP KLIAMLKSPE AKKRMFIPRN QYPEMLVKTL LAIEDKYFYE
     HDGIHLSSIG RAFLVNLMAG RTIQGGSTLT QQLIKNLFLT NTRSILRKIN EIYMALILDR
     FYTKDRILEL YLNEVYLGQD GDEQIRGFPL ASIYYFGRPI NELNLEQYAL LVGMVKGASL
     YSPWTNPNLA LKRRNLVLFL LYKQKYITRK IYKDLCKRSL NVQPKGNIIS SHPSFIQLVC
     EEFHKKIYNP IKNFPGTKIF TTLDYTSQNA VEQAVKIEIP ILKRKKRLKD LEVAMIVIDR
     FTGEVQALIG SSKPEFNGYN RALKTRRSIG SLSKPITYLT ALSQPEKYHL NTWISNYPLS
     IKLDSGQYWT PKNNNFSFSK KVLLLDALIH SINIPTVNLS INIGLKKLVD SWLLLGISKK
     YITPLPSISL GAINLTPFEI AQVFQIIGSG GYKSSLSSVR SIISDDGKVL YQNLPQSIHI
     ESSEASYLTL YGMQQVVKSG TAKSLGTIFK EFSLAGKTGT TNNLVDNWFV GIDGKQIVIT
     WIGRDNNHTT RLYSSSGAMQ IYKRYLQYQR PVPLVLKAPN NINMFYINNL GELFCKKNNQ
     HNRMLPIWSI KNKKICNDKL SERFSIKKKK NFLFWLKNLF
 
 
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