PBP1A_MYCS2
ID PBP1A_MYCS2 Reviewed; 785 AA.
AC A0R7G2; I7GBX5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Penicillin-binding protein 1A;
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=ponA1; OrderedLocusNames=MSMEG_6900, MSMEI_6716;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=20686708; DOI=10.1371/journal.ppat.1001020;
RA Hett E.C., Chao M.C., Rubin E.J.;
RT "Interaction and modulation of two antagonistic cell wall enzymes of
RT mycobacteria.";
RL PLoS Pathog. 6:E1001020-E1001020(2010).
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: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 membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Probably essential. In a depletion mutant growth
CC rate is dramatically impaired, cells are short with bulbous poles
CC and/or rounded internal regions. {ECO:0000269|PubMed:20686708}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP43142.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK70639.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP43142.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011731616.1; NZ_SIJM01000001.1.
DR RefSeq; YP_891100.1; NC_008596.1.
DR AlphaFoldDB; A0R7G2; -.
DR SMR; A0R7G2; -.
DR STRING; 246196.MSMEI_6716; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PRIDE; A0R7G2; -.
DR EnsemblBacteria; ABK70639; ABK70639; MSMEG_6900.
DR EnsemblBacteria; AFP43142; AFP43142; MSMEI_6716.
DR GeneID; 66738154; -.
DR KEGG; msg:MSMEI_6716; -.
DR KEGG; msm:MSMEG_6900; -.
DR PATRIC; fig|246196.19.peg.6721; -.
DR eggNOG; COG0744; Bacteria.
DR OMA; YQLTSMM; -.
DR OrthoDB; 652304at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; 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 Carboxypeptidase; Cell membrane; Glycosyltransferase; Hydrolase; Membrane;
KW Multifunctional enzyme; Protease; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..785
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000421125"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..299
FT /note="Transglycosylase"
FT REGION 392..662
FT /note="Transpeptidase"
FT REGION 605..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..720
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..785
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 426
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 785 AA; 81567 MW; A69C687EC368DF04 CRC64;
MPPDDRLTAV LPPVRDGDIA PPIDVVRAAL EGSPPPKPPP PPPPGRGGGG PSGPGGPSGP
GRQFRINWKW VRRGSAIAVA VMVLLPLITF GMAYMIVDVP EPGDIRTPQV STILASDGSE
IARIVPPEGN RVDVKIDQIP VHVRDAVMAA EDRDFYSNPG FSWTGFLRAI KNNLFGGGGL
QGGSTITQQY VKNALVGDER SGIGGLIRKA KELVISTKMS GEWSKDAVLQ AYLNIIYFGR
GAYGISAASK AYFDKPVEQL DVAEGALLAA LIQRPSTLDP AVDPEGAADR WNWVLDGMVD
IGALSQADRD AQVFPPTVPP DYAFQQNQTT GPNGLIERQV TNELLDLFDI NEQTLNTEGL
QITTTIDPKA QEAAVDAVDK YLEGQDPDMR AAVVSIDPRT GGIKAYYGGS DANGFDFAQA
GLPTGSSFKV FALVAALQQG IGLGYQIDSG PLEVNGIKIG NVEGEGCGTC SIAEALKRSL
NTSYYRLMLK LENGPADVAE AAHDAGVAES FPGVEHTLSE DGKGGPPNNG VVLGQYQSRV
LDMASAYATL AASGVYHKPH FVEKVVNSSG QVLFDASKED NGEERIDKAV ADNVTSAMQP
IAGWSRGHNL AGGRPSAAKT GTVQLGDTGD NRDAWMVGYT PSLSTAVWVG TTEGVKPLVN
KWGSPIYGSG LPSDIWKATM DGALEGTDVE SFPKPTEIGG YAGVPQAPAA PPPSAGPPTD
PGQPSVTVIQ PTIEVAPGIT IPIGPPTTVP VGPPPGAPGA PVGPGAPEVP VAPGAPGVPG
APPPP
