ID A0A023D7M3_ACIMT Unreviewed; 622 AA.
AC A0A023D7M3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 18-JUN-2025, entry version 45.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=Amme_075_022 {ECO:0000313|EMBL:GAJ29705.1};
OS Acidomonas methanolica NBRC 104435.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Acetobacterales; Acetobacteraceae; Acidomonas.
OX NCBI_TaxID=1231351 {ECO:0000313|EMBL:GAJ29705.1, ECO:0000313|Proteomes:UP000019760};
RN [1] {ECO:0000313|Proteomes:UP000019760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB58 {ECO:0000313|Proteomes:UP000019760};
RX PubMed=24330138; DOI=10.1111/1574-6968.12357;
RA Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA Matsushita K., Azuma Y.;
RT "Draft Genomic DNA Sequence of the Facultatively Methylotrophic Bacterium
RT Acidomonas methanolica type strain MB58.";
RL FEMS Microbiol. Lett. 351:9-13(2014).
RN [2] {ECO:0000313|EMBL:GAJ29705.1, ECO:0000313|Proteomes:UP000019760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB58 {ECO:0000313|EMBL:GAJ29705.1,
RC ECO:0000313|Proteomes:UP000019760};
RA Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA Matsushita K., Azuma Y.;
RT "Draft genomic DNA sequence of the facultatively methylotrophic bacterium
RT Acidomonas methanolica type strain MB58.";
RL FEMS Microbiol. Lett. 351:9-13(2014).
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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:GAJ29705.1}.
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DR EMBL; BAND01000075; GAJ29705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A023D7M3; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000019760; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR050396; Glycosyltr_51/Transpeptidase.
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 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019760};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 17..180
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 247..463
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 538..611
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 622 AA; 66705 MW; 63813C7B15BD394A CRC64;
MQASDHTPLD AHTSSDGMWR LPVTSSDVDP AYLALLMATE DRRFDEHPGV DPQALLRAVW
QLARRGHIVS GGSTLAMQTA RLLTPHRHTW TGKLRDMLRA LQLEWRFGRR GVLDLYLTLA
PEGGHIEGIR AASLLYFGHE PGRLSPAEAA ILVTLPRRPA AFWPRRHPEA LMAAARRTLQ
RGGVAPLPIA WPTPDTQGVP HDAPELIGHF LSAGRRGVVT TTLDAHLQRS VRQVLANRTA
PLRGTFATLV ADHDRRILAW VGGAEHPAPG SAIDAVLTPR SPGSTLKPFV YGMAFEKGWM
TPRTRVRDSR LAIGGYAPLD FDHAFRGETT VSEALQLSLN VPAIQALEKI GPTRFQERLS
TNGVPLHLPK TPDGTQTAPS LAIVLGGVGL SLRDLTTLYA ALDHGGRVAP LRVESGGTAP
ETRLLSPRAA ADIRAILRDT APPEGVTNWG DVAFKTGTSY GYRDGWAMAS TPRATIGVWA
GRPDGTASPG LTGRDTAGPV LADVLSLLAP APTREEAPQV EPHRALAALS PALRALPHGR
APQIIFPRDR AEIESRSSDG SMVPVGLEGA GGHPPYRWYV NGIPLNVPPG AQPAWTPDAP
GFAHITLADA GNAHATIDIR VR
//
