ID A0A212TUU0_9ACTN Unreviewed; 886 AA.
AC A0A212TUU0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN06272741_3652 {ECO:0000313|EMBL:SNC69783.1};
OS Streptomyces sp. 2114.4.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938836 {ECO:0000313|EMBL:SNC69783.1, ECO:0000313|Proteomes:UP000198141};
RN [1] {ECO:0000313|Proteomes:UP000198141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2114.4 {ECO:0000313|Proteomes:UP000198141};
RA Varghese N., Submissions S.;
RL Submitted (JUN-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; FYEY01000001; SNC69783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212TUU0; -.
DR Proteomes; UP000198141; 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:SNC69783.1}; 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 137..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 181..362
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 470..726
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 93049 MW; 6952DE5877937B1B CRC64;
MSEHRRKPPQ PQSGGRAAAR RAAQQPPGRR AASPRGSAAD PASHSAPTGH EPGQGGRAEA
RRAAQRGGRR RATDTSVAAA GGGAAGRGGG GRRGGGGDGP DGGRGRGSGK PAKKRLIDYP
RANRVGWRRF VPSWKQVATL CVGFIGLIVG ASGVALALVQ VPDESLAAKS QNNVYLWANG
KVMARDGETN RQNVNITEIP SSMQNAAIAA ENASFRTDSG VDPMGIARAV FNMAKGGETQ
GGSTITQQYV KNAMLSQQQT LDRKFKELFI AIKVGWSKNK NEILQGYLNT SYYGRGAYGI
QAAAQAYYGV DAAKLNANQS AFLATVLKGA DLYDPAGGTS PGATRAANTA RAKARWSWIL
DREVENHLLS KTQRDKYRGH FPTPHLPKPV ASKSGQIGYM MDTAKKYVLK HAGLSEAQFD
KGGYTIRTTF DAKKTNALES AVKKVNKRYI DPKKRAKDKY VQFGGASVVP GDGKIVALYG
GEGYDKGHFS NNADTFGVPV GSTWKPFVLA AGMKYGTARS NGPISPDSRY NGDDHLKVKN
ADGSFVTKRD NSPFYQENES NHPWGYIPLT KAMEQSVNTP FVQLGMDVGM KRVRDMAQAA
GIAPASFDKN LNPSFALGTS TPSAIRMADA YATFAQSGQK VEPYSVTKVT FEGEDLPGFD
KPKQETAMSS NIANNVTKVL ENVIQNGTGK LAKRLNMPAA GKTGTTDENK SAWFVGYTKQ
LSTAVSMFRE DAQNPRQLSM NGVGGFDSIH GGALPTEVWT EYMLQAMKGV TGEPFPAATP
IGRRVDEAGM PTPTPTPTPS DTPSQTPSGT PSDSASPSDS PSPSPTDTCS PWDINCKNSG
GAGNGGANGG GPGGPGGPGG DTGGTSPTPD PTDANGGGGL FGGPSG
//