ID A0A1U6IHR1_9MICC Unreviewed; 768 AA.
AC A0A1U6IHR1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN06272721_107169 {ECO:0000313|EMBL:SLK07512.1};
OS Arthrobacter sp. P2b.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1938741 {ECO:0000313|EMBL:SLK07512.1, ECO:0000313|Proteomes:UP000189995};
RN [1] {ECO:0000313|EMBL:SLK07512.1, ECO:0000313|Proteomes:UP000189995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P2b {ECO:0000313|EMBL:SLK07512.1,
RC ECO:0000313|Proteomes:UP000189995};
RA Peterson S.W.;
RL Submitted (FEB-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};
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DR EMBL; FVZL01000007; SLK07512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U6IHR1; -.
DR STRING; 1938741.SAMN06272721_107169; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000189995; 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 ECO:0000313|EMBL:SLK07512.1}; 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 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 77..264
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 483..645
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 714..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 80789 MW; 3C66AAA0DF22718A CRC64;
MATRKNPLFD TATTLGKILV FLGVSAICGV LVAGLLVPAA AVSGSAASGS IEFFDTLPAE
LKVDPPNQTT RILAADGSEI ASVYTENRTK VALDQISPFV KEAVIAVEDS RFYDHGGVDT
TGILRALVST ARGNRQGAST ITQQYVNNVL NANLAAEGNE DQIKLNGVNK GVGDKLREMK
LAIALEKEFS KEQILEGYLN IVFFNRDAYG IEAASRFFFS TSSKDLTLPQ AALLAGLVNS
PSAFDPISNP ESSKQRRDLV LGLMRDQGKI TQADYDAAVA TPVETKVTQP KQGCAYASTA
PYFCDYVLHL LENNPAYGAE LDERKRLIYG GGLTITTTLD PSAQAAAQEQ VNASAGANPD
KWGAAMVSVQ PNSGKIVSMA QNTTFLPAEG SFDSQVNFNV DKLDKDGNDL NGLGGAQPGS
TMKPFTFAQW LNEGKSMNTV VNAAQRKYPL NFRWRNSCGV VTGAYNTAEK GLGAADDLQN
AEPQWYRPLS VLEGLYNSIN TVTFASAAQL DFCGIQKIVD AVGLHGGLPA DGDPNPKINM
STLANLLGST QTAPLTMASA FATFANDGKY CEPIAITSVK DQTGATLPAQ STNCRDAIKP
EVARGVNYAL QETLNRGSGS LIQPRISTRT SFPIGAKTGT SNNNGSTWVV GHTTGLATAA
WFGDALGSQQ RPGQNVTVNG KFYQGIDGYM IAGPMFSNFM TRIAPAYGTE PFPAPPSNLL
GGGGTTRNTT PATTAPQATQ APAPSSPAAT QPAPEPSSNG NGNGNGNG
//
