ID A0A200HC69_9ACTN Unreviewed; 714 AA.
AC A0A200HC69;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BHE97_08505 {ECO:0000313|EMBL:OUZ10154.1};
OS Aeromicrobium sp. PE09-221.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1898043 {ECO:0000313|EMBL:OUZ10154.1, ECO:0000313|Proteomes:UP000195423};
RN [1] {ECO:0000313|EMBL:OUZ10154.1, ECO:0000313|Proteomes:UP000195423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PE09-221 {ECO:0000313|EMBL:OUZ10154.1,
RC ECO:0000313|Proteomes:UP000195423};
RX PubMed=28218694;
RA Matobole R.M., van Zyl L.J., Parker-Nance S., Davies-Coleman M.T.,
RA Trindade M.;
RT "Antibacterial Activities of Bacteria Isolated from the Marine Sponges
RT Isodictya compressa and Higginsia bidentifera Collected from Algoa Bay,
RT South Africa.";
RL Mar. Drugs 15:E47-E47(2017).
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:OUZ10154.1}.
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DR EMBL; MIJB01000015; OUZ10154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200HC69; -.
DR Proteomes; UP000195423; Unassembled WGS sequence.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000195423};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..42
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 43..714
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013256170"
FT DOMAIN 79..261
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 360..616
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 673..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..697
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 75666 MW; EB711D912834FDA0 CRC64;
MKKAAQTQPK AGSTSSALFS IARLSALAGL IVAAVAVPAA TAATMTTREV TRDVMDLPLT
LEDVPNPQTT ELFASNGDRL AYFYEENRQD IPLDEIAPVM QDAIIAIEDY RFYEHGALDL
QGTLRALVNN TGGGSTQGGS TLTQQLVKLT TLQQATTAEQ RAAAVEATVA RKVRELKLAI
NFEEKYTKDE ILERYLNIAY FGSGAYGVNA AAQRYFSVSP AELTAGQAAL IAGLVQNPVQ
FDPRVYPERA LQRRNTVLAV MAQRGKISAE EATQLSEEPL GLNETEFANG CYGSVAAFSC
DYIQRLLLEE PALGDTRDER LRQLQRGGLT IKSNIDIGMQ NAANAAAADH VDPTDQAIGA
LAMIEPGTGK VRALAQSRPM GDDAEAGQSY LNYTVPKQWG DANGFQAGST FKMFTVAAAL
RKGIPVSKSY NSPQTMTMPA GSYFTCEGNG VGPWPLANST GSGTFNMYTA TRQSVNTYFS
QLERDAGLCE TVSMAEAMGI QVPDRDKVGP FTLGATDVSP LDLAAAYAVP ASGGMYCKPQ
PIDEILDRQG NVLKKYEPEC DRVLTDEEAA QINDILRGVQ EPGGFGHQTA GLSIPSAAKT
GTTNDTMSVT YAGYTPELAT AAIIAGANQA GQPHDLRGIV IKGRVPGGIA SGSGLAGPMW
GQAMRAIQGQ LAPVDFAPPP RRQPANRPPP RPEAPAPQPD NGGDNGGDDG GDDD
//
