ID A0A512MEM4_9BACT Unreviewed; 748 AA.
AC A0A512MEM4;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=BGE01nite_41320 {ECO:0000313|EMBL:GEP44841.1};
OS Brevifollis gellanilyticus.
OC Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
OC Verrucomicrobiales; Verrucomicrobiaceae.
OX NCBI_TaxID=748831 {ECO:0000313|EMBL:GEP44841.1, ECO:0000313|Proteomes:UP000321577};
RN [1] {ECO:0000313|EMBL:GEP44841.1, ECO:0000313|Proteomes:UP000321577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108608 {ECO:0000313|EMBL:GEP44841.1,
RC ECO:0000313|Proteomes:UP000321577};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Brevifollis gellanilyticus NBRC 108608.";
RL Submitted (JUL-2019) 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=2.4.99.28;
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:GEP44841.1}.
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DR EMBL; BKAG01000037; GEP44841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A512MEM4; -.
DR Proteomes; UP000321577; 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: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; 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:UP000321577};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 36..198
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 286..498
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 656..742
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 638..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..660
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 82420 MW; D48B984F43B7339E CRC64;
MVYALLPDPG LYPPDFRFSR TLEDRNGKLL HLTLTTDGKY RRHTPLAEIS PDLIEATLEL
EDRHFYRHPG FNPMSLLRAT WGAVSGSARG GGSTITMQLA RLRHDMHTRT AWGKLWQIFR
AVQMERHYTK AEILEAYLNQ APYGGNVEGI GAASLLWCGK GAHDLTLREA VAFAVLPQSP
TRRRPREGDN KSLANAQHRL WERLRQIRGL PADPLDETFT LRELLPVPRE TPHLARRLFS
ESASPDLQMS GIPVHSTIEV EKQRRVESAL SDYIGRKRDV GITNACALLV HAPTREVLAY
VGSSGFLDST IQGQVDGVLA RRSPGSALKP FIYALAMQQG LIHPYTLLRD GQTSFGGYNP
ENFDRQFSGP IAARDALYHS RNIPAVSLAQ RLAHPGLYGF LKSAGVALPR PAEHYGLSLP
LGGAEVSMEE LAAMYCLLAD DGCARPVKFT PGTAAASTAK PLLTPEVRHL TREMMRTREG
EPALDDPGVL WKTGTSHGFR DAWAAGIRGD YVLVVWIGNF NGRANPAFIA RECAAPLLFE
TFRHLRLPRK RETTPPGLTE IDLCAVSGQL PSPMCQHRVR GGFIPGVSPI TPCEIHREVI
IDSASGLRVA RDDGRPGLQR SVQEFWPPEM LELFRKAGVP RKTPPPLEAS AESLSTAETA
QGPKITSPQS ALVYTLQASA SDRQTIPLRA DAAPGVSRVF WFADSRFLGA STPTQPVMWR
AAAGRWRVHV LDDQGRSAAV QVRVEMLP
//
