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Database: UniProt
Entry: A0A2X0KAM6_9ACTN
LinkDB: A0A2X0KAM6_9ACTN
Original site: A0A2X0KAM6_9ACTN 
ID   A0A2X0KAM6_9ACTN        Unreviewed;       669 AA.
AC   A0A2X0KAM6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=DN069_18800 {ECO:0000313|EMBL:RAG84130.1};
OS   Streptacidiphilus pinicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptacidiphilus.
OX   NCBI_TaxID=2219663 {ECO:0000313|EMBL:RAG84130.1, ECO:0000313|Proteomes:UP000248889};
RN   [1] {ECO:0000313|EMBL:RAG84130.1, ECO:0000313|Proteomes:UP000248889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS16-CNU450 {ECO:0000313|EMBL:RAG84130.1,
RC   ECO:0000313|Proteomes:UP000248889};
RA   Roh S.G., Park S., Kim M.-K., Yun B.-R., Park J., Kim M.J., Kim Y.S.,
RA   Kim S.B.;
RT   "Streptacidiphilus pinicola sp. nov., isolated from pine grove soil.";
RL   Submitted (JUN-2018) 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};
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:RAG84130.1}.
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DR   EMBL; QKYN01000072; RAG84130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0KAM6; -.
DR   OrthoDB; 8865355at2; -.
DR   Proteomes; UP000248889; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000248889};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        44..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          89..264
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          443..629
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   669 AA;  71981 MW;  0A56E96BAE2E84D5 CRC64;
     MGPLGRRLGP VGRWLLRVGR RLAWEYPRPG RVGWRRWMPS WRQWLGGAAY LIIALVATTG
     IAFAMTDIPK NLNTFATQQV NVYYWADGTE MARTGPVDRQ AVPLGQIPKP VQWDILAAEN
     ETFYSDDGVS PRGMMRAVYE MIKGGDTQGG STITQQYVKN VYLNQQQTVT RKLTEAFIAI
     KLDSKLSKDQ ILDGYLNTSW FGRGTYGIER AARAYYGVDV SQLNVSQGAF LASLLKGAGM
     YDPAISPDNQ QRAVTRWKWI LDRMVVIHQL TPAQRAQYTT FPEPIQPRLQ GGLTGQTGYL
     VDLATQYVTA HSSVDPRLFD LGGYQIYTTF QKRRVTALAA SVKAASKGLD PAKRPADKDV
     SFGAATVAAD GRILAVYGGP DYVKQGFDDA NTATVPVGTA FTPLVYAAGL TDGVQLQPGG
     SRTPVSGTSV YDGDNKMPVQ TPEGPYWNKD GQLVKINNDG GRSFGKVTLH QAVVDSINGP
     MAQLGMDVGL TQLRGTVEKF GLLPASMGEP VPVFPLGNST PSAIRMADAY GAFPGEGRHV
     EPYSVSRLLF SGHDVGVDRP QPVQVMTADV AHEVDSALTE SVASGAAQGA RLPGVEVAGK
     AGTMLDATSG WFIGYTGQSV TAVTMFHADP NNGLMLPLTG VMGAPAAQPT STVPTRIFAR
     YTRATASLG
//
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