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Database: UniProt
Entry: A0A212TUU0_9ACTN
LinkDB: A0A212TUU0_9ACTN
Original site: A0A212TUU0_9ACTN 
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
//
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