ID M6QJT1_9LEPT Unreviewed; 828 AA.
AC M6QJT1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Penicillin-binding protein, 1A family {ECO:0000313|EMBL:EMN89147.1};
GN ORFNames=LEP1GSC108_0970 {ECO:0000313|EMBL:EMN89147.1};
OS Leptospira weilii str. UI 13098.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1088542 {ECO:0000313|EMBL:EMN89147.1, ECO:0000313|Proteomes:UP000012118};
RN [1] {ECO:0000313|EMBL:EMN89147.1, ECO:0000313|Proteomes:UP000012118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UI 13098 {ECO:0000313|EMBL:EMN89147.1,
RC ECO:0000313|Proteomes:UP000012118};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Chanthongthip A., Lattana O.,
RA Phetsouvanh R., Newton P.N., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA 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:EMN89147.1}.
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DR EMBL; AHNU02000063; EMN89147.1; -; Genomic_DNA.
DR RefSeq; WP_004503865.1; NZ_AHNU02000063.1.
DR AlphaFoldDB; M6QJT1; -.
DR Proteomes; UP000012118; 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}.
FT DOMAIN 109..261
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 447..733
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 791..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 93822 MW; C931CD8CA0048ABA CRC64;
MKQEPVSYFF RFFVIHFRDR ILQRILNSEN PLKQLAKLCA GLLFFNGFLF VFSVKDLWKV
PGSNQYEKPS VLYGINDKNE YEPIAEFYRF SRVVLNIKEL PLEEDGKLNK LIRSFVSTED
NHFYSHWGLD LRGIFRAFMV NLLAGRIKEG ASTITQQVAR LKFLNTERSF LRKAREAWLA
LFLEAVFDKD TLMEIYLNEI PLGHGTIGVG AAARFYFRKD VKDLTWGESA LLASLTTRPT
EFSPLVNPNS SSAKVRVVFK KFVENGVLDI KTAEREYETF SEYYITLNRS PNDSAFGDRL
NRFPYFTEYV RKNLARYIPI TTLYSGGLKI YSTLNIQHQT QAEKALYAGL KNQTAQSNQR
MFTKIDAFDD AYGEIYDLLS MLNDIPEFKF KISKSVRTFN RTWQEDLRDE LGVLNLLSGT
EFLGEAIDWS YRNQQTEDFL LPVEGALISM RPDTGHITSM VGGSGFRSDN QQIRAFQAYR
QPGSAFKPLI YAAAMEYYNQ HPDPKKNITA ASLFSDSPLQ YVLEDGDEWT PSNYTGEYSG
FIKLREALEL SRNSVAVRVL DHTGISNLVP VLEKILQVEN RSIPKNYSIS LGTFEVSPYE
LARAYAVIAS GGKQVFPLSV LYVEDDSGNV IKDFREEASK QERKQILSPE ICFILTSMME
DVIKKGTGTG ATSYGLNRPA AGKTGTTNNF RDAWFAGYSA ELVSVVWLGY DTGTLSMGKG
MSGGVVAAPI WGRFMSNALS REKSKPFHFG ETGIVRKQIC SISGKLPGSH CNQTEEEYFT
KETVPKEVCD DHRGAGFISE PDPPPSHQTQ VKKKQKTNIF QGDDDLIR
//
