ID A0A1N7IR25_9CORY Unreviewed; 806 AA.
AC A0A1N7IR25;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05444817_101352 {ECO:0000313|EMBL:SIS39517.1};
OS Corynebacterium appendicis CIP 107643.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1161099 {ECO:0000313|EMBL:SIS39517.1, ECO:0000313|Proteomes:UP000186292};
RN [1] {ECO:0000313|Proteomes:UP000186292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44531 {ECO:0000313|Proteomes:UP000186292};
RA Varghese N., Submissions S.;
RL Submitted (JAN-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; FTOF01000001; SIS39517.1; -; Genomic_DNA.
DR RefSeq; WP_076598307.1; NZ_FTOF01000001.1.
DR AlphaFoldDB; A0A1N7IR25; -.
DR STRING; 1161099.SAMN05444817_101352; -.
DR Proteomes; UP000186292; 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 ECO:0000313|EMBL:SIS39517.1}; 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 88..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..312
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 405..658
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..790
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 85386 MW; 456F0526A9BAB915 CRC64;
MARDRDKESG NGSGKKPDAP RRETAKKTDA TRSGAGKQNH TASKANSKAG SKAGAGSTAK
ASAKTEATSG KRTAENAGKN EQSRKSQWLA AFVLALVLIM AVPLTIFGVK YAQADLPQPG
EMETAQVSTI FANDGATQLA RIVPAEGNRE QIPLDEVPEH VQDAVLAAED RDFWENSGFS
FTGFGRAVLG QLTGDDSAGG GSTITQQYVK NTIVGNERSY QRKFNELVYS IKMTRHWSKE
EILAGYLNTI YFGRNAYGIQ AAANAYFDKP ASELTFEEGA VLAGLIQLPS QLDPWNNEQE
SMNRWNYVLD GMVGMGSITP EERAGAKFPD TRDPQSYSAY TEATGPNGLI KNQVMAELEQ
VGITEADVTN RGLQITTTID QRTQDQVLKT SEEQLSLLQE DARAGVVAMD PATGAIKGYY
GGDDPSGWDY ANAGLQTGSA FKIFGLAAAL QQGIPLSAYY DSSPVTVGDR TIDNNSGVYG
GVTTLAEALK KSYNTSFIRM QSDLDNGPLD TADMAHALGV ARELPNIPHT LTENGETPYD
GIILGQYQSR VIDLATGVAT LTNRGVWHPP HFVQRVTTAD GEVLYEFDPE YKERRVNAHV
ADNVIEAMQP IAGWSNKALA GGRPSIAKTG TAQMGDSGNN KDAWMIGGTP QLSVAVWVGT
ADNTSPIFNQ WGGNMYGSMS PGAIWKGVLD GVLEGQEYEQ FPEAKPINWG INPYSGGKYG
GGTAPSYQSY DYGTVTGTGQ GGTGTGQGGA AEAPAPEALA EPAPAPEAPA PAPAPAPAPA
PAPAPAPPAQ RQPEVDIGGL IDELVG
//
