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Database: UniProt
Entry: W1Q4L9_ABIDE
LinkDB: W1Q4L9_ABIDE
Original site: W1Q4L9_ABIDE 
ID   W1Q4L9_ABIDE            Unreviewed;       703 AA.
AC   W1Q4L9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=GCWU000182_000453 {ECO:0000313|EMBL:ESK66111.1};
OS   Abiotrophia defectiva ATCC 49176.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Abiotrophia.
OX   NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK66111.1, ECO:0000313|Proteomes:UP000019050};
RN   [1] {ECO:0000313|EMBL:ESK66111.1, ECO:0000313|Proteomes:UP000019050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK66111.1,
RC   ECO:0000313|Proteomes:UP000019050};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUN-2013) 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:ESK66111.1}.
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DR   EMBL; ACIN03000003; ESK66111.1; -; Genomic_DNA.
DR   RefSeq; WP_023391105.1; NZ_KI535340.1.
DR   AlphaFoldDB; W1Q4L9; -.
DR   STRING; 592010.GCWU000182_000453; -.
DR   GeneID; 84816551; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_2_9; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000019050; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 6.20.370.110; -; 1.
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   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 2A; 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:UP000019050};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          74..243
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          343..590
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   703 AA;  77777 MW;  15A399D0F2572097 CRC64;
     MASQTSFRSR LWQGFKGIWR YYRGWKWLIL IGMSIMLVMS TYLVFIAKTT NVAMLQDALK
     TVTTIYDKND QEAGTLSAQK GTYINLDQMS TTIREAVVAT EDKRFYQHNG FDAQGIGRAL
     VRFVINRNTS GGGGSTLTQQ LVKNAFLTLD QTLQRKLKEF FLALEVEKQF SKDQILEMYL
     NHAYFGNGVW GVEDASQRYF GHSAASLSWN EAAVLTGILK GPSLFNPIDD YEAAIERRNV
     VVGLLEQESV IDSQTAQSIK SSGIELHDAY VAKEQDQYPA YFDAVLDEAV AETGIPEADL
     LAKGYKIYTY LNPEYQNALD SAYQVQGIFP DDNTGTPLVQ SASVVVEPST GGVMAIYGGR
     GDYVHRGFNR ATDMRRSPGS TIKPLAVYEP ALEAGYKINS QVPDQVRAYG NNHYAPENYD
     RQTDPSGQVP LYYALAQSKN TSAVYLMDQL GIGKSVQKLD QFGLKIQAQD QQLTLALGAL
     RQGVSPLQMA SAYAAFANKG IRNDSYLIRQ IKDASGHIIY QNTRPTKYMV MTPRVAADMT
     SMMLETFGGN GTGYGAGPSF GQIAGKTGST EVSDGNMQTR DKWMIGYTPD FVIASWVGLD
     KSGEQSLDDL MPNGMRQLFS IQTTNLMSAS PQTSFGLEMA SQMTTDSNPI ADAVQHYNVG
     ETIDQGAKWV NQNAGNLWDD IVFTTKEAVR GVGDWWRSID WPF
//
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