ID A0A257RRV4_9BACT Unreviewed; 727 AA.
AC A0A257RRV4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=B7X03_01015 {ECO:0000313|EMBL:OYV63647.1};
OS Parcubacteria group bacterium 21-58-10.
OC Bacteria.
OX NCBI_TaxID=1970249 {ECO:0000313|EMBL:OYV63647.1, ECO:0000313|Proteomes:UP000216926};
RN [1] {ECO:0000313|EMBL:OYV63647.1, ECO:0000313|Proteomes:UP000216926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21-58-10 {ECO:0000313|EMBL:OYV63647.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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};
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:OYV63647.1}.
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DR EMBL; NCBF01000005; OYV63647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257RRV4; -.
DR Proteomes; UP000216926; 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: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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..240
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 330..584
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 727 AA; 78349 MW; 5700B1E74E247200 CRC64;
MASRTRLSWR HTILAIFLAL VGLGFLLASA ILIMVALTPV PDINSFSARQ VDQSTKIYDR
TGQVLLYDYN RDAKRSIVPL SDISPNTINA TIAIEDSSFY EHGGIRISSI IRAMLVDAVS
GGLSQGGSTI TQQVVKNELL TNQKSITRKI NEWILAIKME QVYSKNQILE TYLNNIPYGG
TLYGIEAASE SYFGIPAKDV DLAQAAYLAA MIQAPSFYSP YGANRAALDA RKDLVLDRMH
TLGFITDTAY AAAKTEQVSF STGGRNAIIA PHFVFYILNQ LEQTYGPNAL ISGLKVTTTL
DADLQAHAES IIANAAPTLL ANDNASNEAM VAIDPPTGEI LAMVGSSNFF STTTDGQYNA
TLALRQPGST MKPFIYSLAL KDGYTRDTVV FDTPTQFSTS CSPSDVSNST SPCYAPVDYD
GKFRGPMTFE TALAQSINIP AIKVLYLVGI QNAINLAKSF GLTTLGDPSQ YGLTLVLGGG
EVRLMDLTGA YATFANDGVL NPPTGILEVD DSSGTVLAKY TPQPTQVLPA NIARDMSAML
SDNPARVPEY TLDSPLYFPG YDVAVKTGTT DDTRDAWVVG YTPSIAIGTW AGNNDNTPMA
KTIAGMILAP SWHDIMAYAL SKYPKTYFGE PDPISTSVPP MLRGDWRIPD AQGNIMPHSL
LYWTDKNNPQ GSPPSNPSQD PQFSYWEYGV SSWYASHPGL FSGGTMLPVP LSYAATNTVS
TSTAPAL
//
