ID A1AK50_PELPD Unreviewed; 704 AA.
AC A1AK50;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Penicillin-binding protein, 1A family {ECO:0000313|EMBL:ABK97720.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:ABK97720.1};
GN OrderedLocusNames=Ppro_0080 {ECO:0000313|EMBL:ABK97720.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK97720.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABK97720.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00034000};
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:0000256|ARBA:ARBA00023988};
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; CP000482; ABK97720.1; -; Genomic_DNA.
DR AlphaFoldDB; A1AK50; -.
DR STRING; 338966.Ppro_0080; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; ppd:Ppro_0080; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_7; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006732; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase 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; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000313|EMBL:ABK97720.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW Transferase {ECO:0000313|EMBL:ABK97720.1}.
FT DOMAIN 94..267
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 350..622
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 671..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 76715 MW; 4A38C41B18E9CD8C CRC64;
MYPGNGIGEL PRVRADGLSP AAPTCQCTFI THKEYTITVI FTPSLSARKW ICFILLCSFL
LIPAAPLLAR ESFASHPTLP RGYSSIRIFD NQGRFVGRIL PERRYWVSID RIPSFLQKAV
IAVEDARFYE HSGIDVRGIA RALVKDVVKG RMAEGGSTIT QQLIKNRYLS GEKTIDRKLK
EGRMALEFEQ KYTKKQILEM YFNEIYYGNG AWGIAQAARL YFDKNPEQLS EAECSLLAGV
PKAPGVYNPR GKASNVMARR DVVLKRMVEL GMISRGKQQS LRVHPPSVIP PGPAPSYVAH
IRSRLIEQYG AGIVEQGGLE VTTAMDLKLQ KLAEKTLGEG VRRVSPQLQG ALVCLDPANG
DLLAMVGGTG SDGNGYNRAL SARRQPGSAI KPLIFAAAVE NGYTAASIWN DRPESYSSGS
AGTWKPRNYG GERFGDLSLR QALAYSNNVI TVKLLDAVGV PAFTDFAARL GLPLRARHDL
TLALGTEEVT LHDLVLAYAP LANGGSRPKS RSIIRIYDRR HESWTNNPPA LTPVLSPASA
YVTTQMMRDV MVYGTAKSLK KFSLKRPSAG KTGTTDDYRD AWFVGYTPQI ITGIWVGHDK
PRPGGKGFTG GAVPAPIWGR FMDQALASRP AVDFTRPDTV VSVTIDPATG FLATPDCPRK
RVEFFVQGTE PMESCPEHGG SVAAPASVPP VAPASDGQQP VQQP
//
