ID A0A0M2H2K3_9MICO Unreviewed; 945 AA.
AC A0A0M2H2K3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Penicillin-binding protein 1A {ECO:0000313|EMBL:KJL37778.1};
GN Name=ponA1 {ECO:0000313|EMBL:KJL37778.1};
GN ORFNames=RS81_03540 {ECO:0000313|EMBL:KJL37778.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL37778.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL37778.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL37778.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJL37778.1}.
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DR EMBL; JYIZ01000057; KJL37778.1; -; Genomic_DNA.
DR RefSeq; WP_045277377.1; NZ_JYIZ01000057.1.
DR AlphaFoldDB; A0A0M2H2K3; -.
DR STRING; 92835.RS81_03540; -.
DR PATRIC; fig|92835.4.peg.3573; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000033956; Unassembled WGS sequence.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 2.
DR Gene3D; 3.30.10.20; -; 2.
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; IPR005543; PASTA_dom.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF03793; PASTA; 2.
DR Pfam; PF00912; Transgly; 2.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 2.
DR PROSITE; PS51178; PASTA; 1.
PE 4: Predicted;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956}.
FT DOMAIN 796..861
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 835..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 99333 MW; 9440DF084401BD8D CRC64;
MPDTKRTATG VLGGLAGLVG LSAVAGVLVT ATITPAIALS GAAASSAITM FDNLPSELEI
DKLMLPTTIY YKHAQTGETK VLTQFYDQNR SPVTYDEISP VMYDAILSSE DPRYYEHGGI
DLIGTTRAVL SNIKGGAETQ GGSSISQQYV KNILVQRCEA TAKTTAIEEL TAEAEEAAKK
EGVDPVAPTA DEINARRDQV NANCWSAATT AKGNDGIQRK LQEMRYAISL EKKYSKEDIL
LGYLNIANFG GTTYGIDAAA RYYFNVASKD LSVGQAAILA GIVQNPNSYR IDLKDGSIFD
NEGNSYNKAP DGVIDEGADL RVLDSLVESG EITDEQRLEA ADGYTSTKVR QLYVLSRMLE
DGKITREEYV AAAAAPITPE ITRPKDGCAS TGAAAYYCQY VVEVIKNDPA FGETEDDRLK
ALRQGGLKIY TTLDTTVQKA AEVATSTYAP TSISMPTSEG GSTGRFGSTT VSIEADTGRI
LAIAQNTKFS EDASVADDPD FSSLVFAGDT TFGGSTGFNA GSTFKLFTLV DWLEKGNSVN
QVLNGSLRVF PKLTNSCDGD WYNESNTVVN NFAKAPGRIG TPMQFTASSL NTGYFAMAEK
LDLCDIKKVA TKMGVTQANG NEVEMKTLAS IIGTNTVSPI SIAGAYATVA NKGVYCQPQV
IDAIVDAEGE DMAVPERSCT QVIDPKVAAT AAYALQGVMA SGGTGSQGNT WDGTALIGKT
GTHEAWQTWL VESSTKVATA TWAGNVYGHG DVFRTWTDSG YRLSDIRYSI AKATQAAANA
RYAGTAFPAP DTNLSRQVLT DLPNVVGKTV EEATKILTDA GFTVTVGSAV SSSEDKGIVA
EQDPAPGKVS GGATVTISPS NGKGVTVPDV SGRELNKALS MLRNAGFGSV QAGTCVQDED
GGRADRATVT SPAAGSVVNR NTSITVDYTS RDCGAGGGGS DGSDD
//
