ID A0A3N2BD61_9MICO Unreviewed; 789 AA.
AC A0A3N2BD61;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Membrane peptidoglycan carboxypeptidase {ECO:0000313|EMBL:ROR73193.1};
GN ORFNames=EDD31_1565 {ECO:0000313|EMBL:ROR73193.1};
OS Bogoriella caseilytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Bogoriella.
OX NCBI_TaxID=56055 {ECO:0000313|EMBL:ROR73193.1, ECO:0000313|Proteomes:UP000280668};
RN [1] {ECO:0000313|EMBL:ROR73193.1, ECO:0000313|Proteomes:UP000280668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11294 {ECO:0000313|EMBL:ROR73193.1,
RC ECO:0000313|Proteomes:UP000280668};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) 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:ROR73193.1}.
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DR EMBL; RKHK01000001; ROR73193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2BD61; -.
DR Proteomes; UP000280668; 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 SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51178; PASTA; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:ROR73193.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000280668}.
FT DOMAIN 696..761
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 428..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..789
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 84430 MW; E47E5BE2A0F9A84D CRC64;
MLALLLTFVL VAGLGGVLAA GLMLPALGAV GTATQATEDM FDEIPDELAI PEPSQRSEIL
WADGSRMASI YADNRVVVPL DQMNPHLRNA VVAIEDRRFY DHRGVDPEGI ARAFVNNLAG
GSLEGASTIT QQYVKNALIE HGRITGDADL IREAQDESYG RKLAEAQMAI SLEQQLTKDQ
ILEGYLNLAQ FGRSQYGVEA AAQYYFGKPA ADVTPAEAAT LAGITQSPAA HDPERYPEQS
ERRRNTVLSV MRAQGFLSEA EYQEARDTPM EEMLTITPAP NGCQAARSAA YFCEYVVDEL
LQHEEWLDSR EERRDALYRG GLIIHTTLDR ERQVAAYESV TASVPVGDPS NIRMALSSVD
PTTGDIQAMA QNTNFGSPSE EDSSATSVNL NVGLSHGGGR GFQGGSTHKV FALIEWLREG
GALEDTITVR SPTGPDGRRE FEPDEWSNSC DAANPGSVYP PRNIEGTGSD VMTVHDATRM
SINLPFVEMA TQIDLCAMMD TAAAMGLERA DGNPLLNYPS TVLGSNEITP LSQAVAFGTL
ANDGIACAPR AITSIENHHD EELATFETSC ERALESSVVN AANHSLQAVI DDDPYATGRS
AILPEGRSAA GKTGTANDAS ASWFVGYTPE QLSTAVWMGY QEATGAMTNV TVDGQHYDWI
FGSHIPAPTW RDYMARALDG EPQTRFGEVG ERELEGERRR VPSVTGQSIG QAEDTLEQAG
FSTRVGSGQY SSAPFGTVAG TSPGGGTEVR GAELITIHPS AGPPPASTNN TGGDDDDGDD
SEDSDGDED
//
