ID G2GCW9_9ACTN Unreviewed; 1008 AA.
AC G2GCW9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SZN_16730 {ECO:0000313|EMBL:EGX58632.1};
OS Streptomyces zinciresistens K42.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX58632.1, ECO:0000313|Proteomes:UP000004217};
RN [1] {ECO:0000313|EMBL:EGX58632.1, ECO:0000313|Proteomes:UP000004217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K42 {ECO:0000313|EMBL:EGX58632.1,
RC ECO:0000313|Proteomes:UP000004217};
RA Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL Submitted (AUG-2011) 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:EGX58632.1}.
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DR EMBL; AGBF01000049; EGX58632.1; -; Genomic_DNA.
DR AlphaFoldDB; G2GCW9; -.
DR PATRIC; fig|700597.3.peg.3279; -.
DR Proteomes; UP000004217; 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:SF34; PENICILLIN-BINDING PROTEIN 1A; 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:UP000004217};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 247..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 293..467
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 570..826
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 105858 MW; 1D2105E630A68DEC CRC64;
MHDMSDESQP QPKAQAHPDR DPEPEAVAQP EPEREPEPRA EAQPDREAEA RPKPGARPEP
EPKAEAGPAP DRAPEPEPKA GPAPAAAPGP KAGPSADRTP GPKAGPRPDL RWQARAEAPP
APGPRPGTEP ESDPDPMERT QALRRPKAPP APAPGAEATA GTQSPAHSRP PTPPPAQAYT
QAQPQSQAQT QAQPQTQGHA QGHAQAPAQT QAQSQIQPET QARQESGGKP RRPKRTGWRR
LVPTWRILLG TFVIGVLLLG GVFFLAYSLV KIPPANALAT KQANVYLYSN GSVIARDGEV
NRENITLAQM SKASRYAILA AEDRDFYTES AIDPKAMLRA AWNTATGKGK QSGSTITQQY
VKNYYLRQEQ TVTRKAKEFI IAVKLDREKS KNEILEGYLN TSFFGRNSYG IQAAAQAYYG
MDAKDLDPAR AAYLAALVNA PSEYDVVARP ENKEAVLARW NYVLDGMVKK GWLGASERAG
LKFPMPKETA TSTGLSGQRG YIVQIVQDHL IKNRIVAKEE LDRGGYRITT TLQKDKQDAF
VDAVNDKLIS RLDKKNRKVD NYVRAGGASV DPKTGKVVAM YNGIDYVKQY TPNATRRDFQ
VGSTFKPFVF TSAVENGSTT QDGRTITPNT VYDGTDKRPV QGWSGGSYAP GNEDDVSYGN
VTVRAATDKS VNSVYAQMAV DVGPDKVKKT AVALGLPAAT PDLQPYPSIA LGTATASVLD
MAEAYATLAN NGKHGTYTLV EKVTRDGADV IELPARKTTQ AISREAADTT TSVLRSVVDN
GTATAALAAG RPAAGKTGTA EEDQAAWFAG YTPDLATVVA VMGQDPVTAK HKSLYGVMGL
PRINGGGAPT EIWAQFTKQA LKGKPAKQFD LRLQENANAP QDPTTDPTAG DPSTGGEDGG
ASGQPTPGQD TEGQTGGQTP GEPDGGLTEG GQNGGTGDGG ATDGGTGGES TGGTGDGGTT
DGSTSGGTGS AGTDTGGQTG GTTDGSTNSG GTGTTGTTVG LPGTTRRE
//
