ID M3GWJ6_LEPBO Unreviewed; 824 AA.
AC M3GWJ6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Penicillin-binding protein, 1A family {ECO:0000313|EMBL:EMF99208.1};
GN ORFNames=LEP1GSC123_4592 {ECO:0000313|EMBL:EMF99208.1};
OS Leptospira borgpetersenii str. 200701203.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193007 {ECO:0000313|EMBL:EMF99208.1, ECO:0000313|Proteomes:UP000011783};
RN [1] {ECO:0000313|EMBL:EMF99208.1, ECO:0000313|Proteomes:UP000011783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701203 {ECO:0000313|EMBL:EMF99208.1,
RC ECO:0000313|Proteomes:UP000011783};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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}.
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:EMF99208.1}.
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DR EMBL; AKWO02000073; EMF99208.1; -; Genomic_DNA.
DR AlphaFoldDB; M3GWJ6; -.
DR BioCyc; LBOR1193007:G11KN-20-MONOMER; -.
DR Proteomes; UP000011783; 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 Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000011783}.
FT DOMAIN 83..261
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 447..731
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 789..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 93248 MW; C03819371482398F CRC64;
MKQEPVSYFF RFFVIHFRDR ILQRILNSEK PLKQLTKLCV GLLFLNGFLF VFSVKDLWKV
PGSNQYEKPS VLYGINDKSE YEPIAEFYRF SRVVLNIKEL PPEEDGKLNK LIRSFVSTED
NHFYSHWGLD LRGIFRAFMV NLLAGRIKEG ASTITQQVAR LKFLNTERSF LRKAREAWLA
LLLEAVFDKD TLMEIYLNEI PLGHGTIGVG AAARFYFRKD VKDLTWGESA LLASLTTRPT
EFSPLVNPNS SSAKVRVVFK KFVENGVLDV KTAEREYETF SEYYITLNRS PNDSAFGDRL
NRFPYFTEYV RKNLARYVPI TTLYSGGLKI YSTLNIQHQT QAEKALYAGL KNQTAQSNQR
MFTKIDAFDD AYGEIYDLLS MLNDIPEFKF KISKSVRTFN RTWQEDLRDE LGVLNLLSGT
ESLGEAIDWS YRNQQTEDFL LPVEGALISM RPDTGYITSM VGGSGFRSDN QQIRAFQAYR
QPGSAFKPLI YAAAMEYYNQ HPDPKKNVTA ASLFSDSPLQ YVLEDGDEWT PSNYTGEYSG
FIKLREALEL SRNSVAVRVL DHTGISNLVP VLEKILQIEN RSVPKNYSIS LGTFEVSPYE
LARAYAVIAS GGKQVFPLSV LYVEDDSGNI IKDFREEVGK QERILSPEIC FILTSMMEDV
IKKGTGTGAA SYGLNRPAAG KTGTTNNFRD AWFAGYSAEL VSVVWLGYDT GTLSMGKGMS
GGVVAAPIWG RFMSNALSRE KSKPFHFGET GIVRKQICSI SGKLPGSHCN QTEEEYFTKE
TVPKEVCDDH RGAGFISEPD PPHQTQVKKK QKTNIFQGDD DLIR
//
