ID A0A2A9D4H3_9MICO Unreviewed; 840 AA.
AC A0A2A9D4H3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Membrane peptidoglycan carboxypeptidase {ECO:0000313|EMBL:PFG20749.1};
GN ORFNames=ATL40_2360 {ECO:0000313|EMBL:PFG20749.1};
OS Serinibacter salmoneus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Serinibacter.
OX NCBI_TaxID=556530 {ECO:0000313|EMBL:PFG20749.1, ECO:0000313|Proteomes:UP000224915};
RN [1] {ECO:0000313|EMBL:PFG20749.1, ECO:0000313|Proteomes:UP000224915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21801 {ECO:0000313|EMBL:PFG20749.1,
RC ECO:0000313|Proteomes:UP000224915};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG20749.1}.
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DR EMBL; PDJD01000001; PFG20749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9D4H3; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000224915; 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; 1.
DR Gene3D; 3.30.10.20; -; 1.
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; 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 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:PFG20749.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000224915}.
FT DOMAIN 80..275
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 390..680
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 743..798
FT /note="PASTA"
FT /evidence="ECO:0000259|Pfam:PF03793"
FT REGION 791..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..840
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 89394 MW; B8422C7EE620B2E3 CRC64;
MESPRPTRRH EVNVFQALAL LLAFLLLAVT GGVLTAGLLM PAVAAVGSVS GAAQQLFDDL
PTEVEIAPPS ERSVILAADG STLATFYSEN RVVVPLEEIS PMMQAAVIAT EDERFYDHAG
VDTQGLMRAL FRTLQGDTQG ASTLTQQYIK NVLIEEGRQT GDEEAIEAAQ EADGAEGINR
KLREMKLAIS LEKEYSKDQI LEGYLNIAQF AVGTFGVETA ANYYFNKSAA ELNAGEAALI
AGVTKSPTLY DPTRASDEEY TTATNRRDTV LTQMHDQGYI TDAEYDEAIN TPVADMLDVT
RTTQGCATAG ISAYFCQYVT ASLVNDGYLG ETEEESRQAL QRGGLTITTT IDLERQRQAY
ESLVSQIPTN DPTYNSSVSG VYGVSGAISS VEPGTGNVEA MVQNTTYGEA TEEDPRATTV
NFNVDRAYGG GDGFQTGSTF KAFVLTQWLI DGHSLAETVD ATNGQTFPFE SWNISCSPSS
ASDYEPKNLE GAGGSNMTVL EATRQSVNTA YAYMENQMDL CDLRETTSKM GVHVGTGTIN
PDLLPEGSPA RALYEEQAGE DILAVPSMVL GSNTIAPLTM AAAFATYANE GVYCEPRAIT
AIQDRDGNEI EVPEPQCERA LSEEITAGVN YALQEVVSPG ATGAAAQIDR PVGGKTGTAN
DDMHAWFVGY TPQLSTAVWV GHSEGNISMF NTVINGIFYS QVYGGRLPAP IWASYMSQAL
AGEPAQGFAE ADREQVYGEE LPVPNVRGKN LANATAILEQ AGFRVQIGSN RYGSMPVGLV
EAYSPSGIST RNSTITIYPS AGPAPAPEPE PEPEPSEDEG GDDDGGDDDG GGDGDGDGDD
//
