ID A0A0U1L4U6_9FIRM Unreviewed; 662 AA.
AC A0A0U1L4U6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Multimodular transpeptidase-transglycosylase {ECO:0000313|EMBL:CQR74535.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:CQR74535.1};
GN ORFNames=SpAn4DRAFT_0997 {ECO:0000313|EMBL:CQR74535.1};
OS Sporomusa ovata.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=2378 {ECO:0000313|EMBL:CQR74535.1, ECO:0000313|Proteomes:UP000049855};
RN [1] {ECO:0000313|Proteomes:UP000049855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nijsse Bart;
RL Submitted (MAR-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; CTRP01000014; CQR74535.1; -; Genomic_DNA.
DR RefSeq; WP_021170517.1; NZ_CTRP01000014.1.
DR AlphaFoldDB; A0A0U1L4U6; -.
DR Proteomes; UP000049855; Unassembled WGS sequence.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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 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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000313|EMBL:CQR74535.1};
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:UP000049855};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:CQR74535.1}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..662
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006710771"
FT DOMAIN 50..224
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 303..546
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 627..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 72595 MW; 113556FEFF15E97B CRC64;
MKKTSIRVTI LALLFAMSVN TCFAFLGLPG TDNLNDLNLV AATQVFDING QLISKLFEEN
RIVVTINSMS PYIQQAIIAN EDTRFYNHFG IDPIGIIRAV VVNIRRGSLV EGGSTITQQL
AKNMFLTQER TFIRKVKEAV LALVIDYKFS KQEILQAYLN QVYFGEGAYG VEAAAQMYFG
KHANELTLSE SAVLAGLPRG PNIYSPYVDM KAAIERRAVV LDSMVKAGYI TQQEAARAKV
EPITLAGKKK RVVQASYFLD YVAKELVDRY GADRVYKGGL KVYTTLDISQ QQAAEAVLGQ
MQGAVLALDS KTGYIKAMVG GRNYEESQIN RVFAEVRQPG SAFKPFLYAT AINQGLTANA
IIIDEPININ GYSPLNYDKK YRGPITMKKA LRWSVNIAAV KLGQQIGIDQ VLNLAKTMGI
TTLTPEDNNL ASALGGLTQG VSLWELTTAY TAFANNGVLS KPMAIVKVLD EHGQVLEEGR
IEQQSVLKPD TAYILTDMLR GVLQDGTATP ANLGRPAAGK TGTTDNYETA WFIGYTPDIV
VGIYVGNDNR KPVSISGTEV SALWGKMLSK IVAGMPPADF PIPPNVVVGI PVCTSTGKLA
GSGCRETEYS AFIKGTEPTA PRMNDRIKQW LTPDETQPQP PEQQEQKNQP FWKWPWSRLP
SF
//
