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Penicillin-binding protein 1B (PBP-1b) (PBP1b) (Murein polymerase) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase) (Peptidoglycan glycosyltransferase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)]

 PBPB_BUCAI              Reviewed;         760 AA.
P57296;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 1.
05-DEC-2018, entry version 119.
RecName: Full=Penicillin-binding protein 1B;
Short=PBP-1b;
Short=PBP1b;
AltName: Full=Murein polymerase;
Includes:
RecName: Full=Penicillin-insensitive transglycosylase;
EC=2.4.1.129 {ECO:0000250|UniProtKB:P02919};
AltName: Full=Peptidoglycan TGase;
AltName: Full=Peptidoglycan glycosyltransferase;
Includes:
RecName: Full=Penicillin-sensitive transpeptidase;
EC=3.4.16.4 {ECO:0000250|UniProtKB:P02919};
AltName: Full=DD-transpeptidase;
Name=mrcB; OrderedLocusNames=BU200;
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
(Acyrthosiphon pisum symbiotic bacterium).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Erwiniaceae; Buchnera.
NCBI_TaxID=107806;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=APS;
PubMed=10993077; DOI=10.1038/35024074;
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids
Buchnera sp. APS.";
Nature 407:81-86(2000).
-!- FUNCTION: Cell wall formation. Synthesis of cross-linked
peptidoglycan from the lipid intermediates. The enzyme has a
penicillin-insensitive transglycosylase N-terminal domain
(formation of linear glycan strands) and a penicillin-sensitive
transpeptidase C-terminal domain (cross-linking of the peptide
subunits) (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-
D-Ala)](n)-diphospho-di-trans,octa-cis-undecaprenol + beta-D-
GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
diphospho-di-trans,octa-cis-undecaprenol = [GlcNAc-(1->4)-
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-diphospho-
di-trans-octa-cis-undecaprenol + di-trans,octa-cis-undecaprenyl
diphosphate + H(+); Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602,
Rhea:RHEA-COMP:9603, ChEBI:CHEBI:15378, ChEBI:CHEBI:58405,
ChEBI:CHEBI:60033, ChEBI:CHEBI:78435; EC=2.4.1.129;
Evidence={ECO:0000250|UniProtKB:P02919};
-!- CATALYTIC ACTIVITY:
Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also
transpeptidation of peptidyl-alanyl moieties that are N-acyl
substituents of D-alanine.; EC=3.4.16.4;
Evidence={ECO:0000250|UniProtKB:P02919};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type II membrane protein {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the
glycosyltransferase 51 family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
transpeptidase family. {ECO:0000305}.
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EMBL; BA000003; BAB12917.1; -; Genomic_DNA.
RefSeq; NP_240031.1; NC_002528.1.
RefSeq; WP_010895998.1; NC_002528.1.
ProteinModelPortal; P57296; -.
SMR; P57296; -.
STRING; 107806.BU200; -.
CAZy; GT51; Glycosyltransferase Family 51.
PRIDE; P57296; -.
EnsemblBacteria; BAB12917; BAB12917; BAB12917.
GeneID; 1109643; -.
KEGG; buc:BU200; -.
PATRIC; fig|107806.10.peg.211; -.
eggNOG; ENOG4105BZ4; Bacteria.
eggNOG; COG0744; LUCA.
HOGENOM; HOG000282711; -.
KO; K05365; -.
OMA; VHGMGLA; -.
UniPathway; UPA00219; -.
Proteomes; UP000001806; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008658; F:penicillin binding; IEA:InterPro.
GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
Gene3D; 1.10.3810.10; -; 1.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR001264; Glyco_trans_51.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR011813; PBP_1b.
InterPro; IPR036950; PBP_transglycosylase.
InterPro; IPR001460; PCN-bd_Tpept.
InterPro; IPR028166; UB2H.
Pfam; PF00912; Transgly; 1.
Pfam; PF00905; Transpeptidase; 1.
Pfam; PF14814; UB2H; 1.
PIRSF; PIRSF002799; PBP_1b; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF56601; SSF56601; 1.
TIGRFAMs; TIGR02071; PBP_1b; 1.
3: Inferred from homology;
Antibiotic resistance; Carboxypeptidase; Cell membrane; Cell shape;
Cell wall biogenesis/degradation; Complete proteome;
Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 760 Penicillin-binding protein 1B.
/FTId=PRO_0000083185.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 760 Extracellular. {ECO:0000255}.
REGION 136 308 Transglycosylase.
REGION 392 684 Transpeptidase.
ACT_SITE 174 174 Proton donor; for transglycosylase
activity. {ECO:0000250|UniProtKB:P02919}.
ACT_SITE 451 451 Acyl-ester intermediate; for
transpeptidase activity.
{ECO:0000250|UniProtKB:P02919}.
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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