ID A0A1M4ZL72_9BACT Unreviewed; 819 AA.
AC A0A1M4ZL72;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05444362_104124 {ECO:0000313|EMBL:SHF18830.1};
OS Dysgonomonas macrotermitis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=1346286 {ECO:0000313|EMBL:SHF18830.1, ECO:0000313|Proteomes:UP000184480};
RN [1] {ECO:0000313|Proteomes:UP000184480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27370 {ECO:0000313|Proteomes:UP000184480};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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};
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DR EMBL; FQUC01000004; SHF18830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M4ZL72; -.
DR STRING; 1346286.SAMN05444362_104124; -.
DR Proteomes; UP000184480; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000184480};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..260
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 338..588
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 726..816
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 819 AA; 93830 MW; 18DCFDAC00C93644 CRC64;
MVQRGVRKNT IDILKTKLIF RLRFYFTIYR MKRFFLKWID RYRTAKLKYR ISIPVMLILS
IWYIFCLPSP LFDVPYSTVV SDRHEELLGA RIADDQQWRF PTVDSVPEKY KTCLIEFEDQ
YFRYHWGINP GSILRAVKQN FSEKRIVSGA STITMQTIRL ARKENRTFGE KFLEMIMATR
LEFSYSKDEI INLYASHAPM GGNVVGIEAA SWRYFGHQSS TLSWAEAATL AVLPNSPAMM
HFGRNRSKLL SKRNNLLKKL YEREILDKTD YELALAEPLP FEPYALPQIA PHLVTKIYKE
QGGKQIRTTI DKQRQLLIEN ILSRWNAEFA QNEIKNIAAI VIDVEKNEVI AYCGNVHFDK
SISANQVDIL QSPRSTGSIL KPFLYCAMMD NGQLLPNQLL ADIPININGF TPKNFSLNYD
GAVPASEALA RSLNIPFVTS LRKYGVTKFY NLLRDAGMTT LSRSPDNYGL SLILGGAEGK
LWDISQMYAH MAQSLNDYNR EQSYWKRKPV SYIYDEDNDK TEEHITDPLF KAGAIWLTLD
ALTNLNRPEE IDWRSIPSIQ KIAWKTGTSF GFRDGWAVGV NPKYTVGVWV GNSDGEGRPG
LTGARTAGMV MFDIFNALPS SKWFTAPIRD LVKTEVCRES GFLTGVNCPE SSKDTLWVTK
KALEAPVCSY HIKVNVSEDF KYRVYEDCAG GRGIVQTSWF VLPASWEWFY KEHHPSYRSL
PPFSPECQAD DNTKVMEFIY PVNNAVVSIP KQLDGTQGRI IFELAHRNPQ SKVFWHLDED
YIGETQNFHK KELSPLKGNH RLTVVDEAGN SVSIRFIVK
//