ID A0A0A7KDS0_9DEIO Unreviewed; 791 AA.
AC A0A0A7KDS0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:AIZ44281.1};
GN ORFNames=QR90_02875 {ECO:0000313|EMBL:AIZ44281.1};
OS Deinococcus radiopugnans.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=57497 {ECO:0000313|EMBL:AIZ44281.1, ECO:0000313|Proteomes:UP000030634};
RN [1] {ECO:0000313|Proteomes:UP000030634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter sp. DG25B genome submission.";
RL Submitted (NOV-2014) 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; CP010028; AIZ44281.1; -; Genomic_DNA.
DR RefSeq; WP_039682100.1; NZ_CP010028.1.
DR AlphaFoldDB; A0A0A7KDS0; -.
DR STRING; 1182571.QR90_02875; -.
DR KEGG; dsw:QR90_02875; -.
DR HOGENOM; CLU_006354_2_4_0; -.
DR Proteomes; UP000030634; 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: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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030634}.
FT DOMAIN 65..240
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 355..640
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 746..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 87196 MW; ECDF95CC005249D3 CRC64;
MIFFVRFLKF LTSFLIAALF AGAGVAATYG LKWWRELPDY RQLDSLSLGA ETRVFARDNT
PLGTLIPKIG EQAISRTLVN LNEISPFMVA ALVSNEDRRF FEHYGIDPYG LGRQVQRLAA
GDSVQGGSTL TNQLIKNTLL LDEYQQARTP DRKIKEWLLS VQVERSFTKA EILQNYLNTI
YWGDGGPVEL YGIYSAAQAY FRTTPKDLTL AQSAYLTVLV PSAGRYFDYK AMRPLMKTLL
GRMVEDKWIT PAQMDAALKE DLQPRGWKVL YDKQGRITSA KLVDRTQKEL KAVTTVRYPH
FMRQVEQELV QRFGRDKVYG SGGLRVYTTV DPRVQAAVET ASREATGLPP GATLAATIVD
PFTGEVLGMI GQKLNGSAPP EAWNNAAQGQ RQIGSTIKPL LYTTALSTGL TQEHREDDKP
YSSPCATCKG GVYEPQNFEG QTTYRTMTIR EALDRSLNLV TVRLADRIGL QTFFGKLREL
GIPPNDGTGL AAALGAVETT PVKMAAAYAP FANGGLYRAP RYLTRVTTAR GEVLYDDGLN
PVKPTRVWTP QIAWLGLDMI RGVVNDLSAA QGGLAWPAKF GDWPVAGKTG TSNGPKDLWF
VGTTPLYTGA VWVGKQQGGE MPINSYSGLV NGPIWRRMME LAHQGQTVRA FSEPPGIQYV
DAPDQQFLPG VKLAVLDPNY SDAANTALQE NAPPPVQYTE SRYTSAYNDP RTVLIDVDRT
TNRQATEFTP PENIVQRRVY IEQLPAYAPD DSPAPLTDEK ADPAAVKAVR NQNAVPQIPE
PKSAAPQPAK P
//
