ID A0A2L0F0M7_SORCE Unreviewed; 744 AA.
AC A0A2L0F0M7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Penicillin-binding protein 1A {ECO:0000313|EMBL:AUX45019.1};
GN Name=pbp1a {ECO:0000313|EMBL:AUX45019.1};
GN ORFNames=SOCE26_065000 {ECO:0000313|EMBL:AUX45019.1};
OS Sorangium cellulosum (Polyangium cellulosum).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=56 {ECO:0000313|EMBL:AUX45019.1, ECO:0000313|Proteomes:UP000238348};
RN [1] {ECO:0000313|EMBL:AUX45019.1, ECO:0000313|Proteomes:UP000238348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce26 {ECO:0000313|EMBL:AUX45019.1,
RC ECO:0000313|Proteomes:UP000238348};
RA Zaburannyi N., Bunk B., Overmann J., Mueller R.;
RT "Sorangium comparison.";
RL Submitted (SEP-2015) 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; CP012673; AUX45019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L0F0M7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000238348; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; 2.
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 InterPro; IPR003029; S1_domain.
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.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 331..403
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 744 AA; 79472 MW; 6665B7B5C6AD484D CRC64;
MAASTLLGLG LLAFAALIWH YGQDLPRTSE LKSYRPPEVT RILARDGTPL AELFVERRTV
VPISVVPNSM KLAVLAAEDA NFYKHEGLNY VGILRALLVN LRSAQARQGG STITQQVIKN
VLLTPERTFA RKIRELILAR RIEQELTKDE ILELYLNHIY FGHGRYGVEE AARYYFGKSV
RDVQLAEAAL LAGLVKGPSV YSPRVDLARA EERRSYVLHQ LGDKGFASRT DVDAAARQKI
VLAPPPEHAA ELAPEVVAEV ERALVAAVGP QANRGGYTVT TTIDPKLQAA ARAAVRGNLD
AYAARRGLIA PLKRGKGDPA PFEGAPTQGS GRIYQGVVTK ADDVAGTLTV RVGTAEGVVK
LERAARYNPR KLPPSQFAEI GKVVRVTFDG GDPRGGRLEL ALGPQSALVA LDVRTAEVLA
VVGSYDAVRG ALNRARSARR QPASTFKPIV YSYGIHTRAF TAASILETQP AALGGKYRPD
NYDESDGQAP RRLREALASS VNVAAVWTLE QLGPAKVAEW ARSLGITSKL GADLSLALGA
YEVTPFEMVA AFNTFAAGGT YRDPVLVRSI IGPGGQPLPL PSATPARQVM SEAEAYIMTS
LLRSVVESGT AKRARSMSTP VAGKTGTSNA AKDAWFVGYS TDIACAVWTG HDDASPLGPG
ETGGATSLPA FMAFMQDAHK ARPRTDFAAP PDGLVRVLID TATGRLAPPG AAGAIEEVFL
AGTEPTTYAE PSWSGEAPRI EWPF
//
