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Database: UniProt
Entry: A0A238WDD9_9FLAO
LinkDB: A0A238WDD9_9FLAO
Original site: A0A238WDD9_9FLAO 
ID   A0A238WDD9_9FLAO        Unreviewed;       776 AA.
AC   A0A238WDD9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN06265376_101955 {ECO:0000313|EMBL:SNR44437.1};
OS   Dokdonia pacifica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Dokdonia.
OX   NCBI_TaxID=1627892 {ECO:0000313|EMBL:SNR44437.1, ECO:0000313|Proteomes:UP000198379};
RN   [1] {ECO:0000313|EMBL:SNR44437.1, ECO:0000313|Proteomes:UP000198379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25597 {ECO:0000313|EMBL:SNR44437.1,
RC   ECO:0000313|Proteomes:UP000198379};
RA   Kim H.J., Triplett B.A.;
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};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; FZNY01000001; SNR44437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238WDD9; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000198379; 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; 2.
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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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:UP000198379};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..249
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          439..694
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   776 AA;  87832 MW;  126A60235B6B7679 CRC64;
     MAKKQIKKKQ ATSTQPNFKK FIKWFWGLFA GGLLAVVLLF LLASWNVFGK LPTFEELENP
     ESNLATKILS VDGKQLGTYY NENRTPIKYE DLPQHLVDAL VATEDERYFD HSGIDFKGTA
     RAFAFLGSRG GASTVTQQLA KLLFSDTPRS TPERLIQKVK EYVIATRLER QYTKEEIITM
     YLNKQGFLFN AIGISSASRI YFNKNVSDLS IEESAVFVAM LKNPRQFNPH RKISREKSKR
     RRNQVFKQME KNGFLTTAEK DSLQALPMVV RFTPEGHRDG MATYFRENLK KFLADWIKKN
     PKGEDDDGNL EYYNIYRDGL TITTTIDSRM QQMAEEAVKK HMPRLQAEFD KQNIKNKIAP
     FRDIEESEIE TIFNNAIKSS ERWRKMKAAG KSESDIRKSF DIKTDMSIFS WQGDIDTVMT
     PRDSIRYYKK FLRTGMMSMV PQTGEVRAWV GGINMSHFQY DHVQTGKRQV GSTFKPFLYA
     TAVDQLHISP CDTLPNTLFC IAEGKMGNTK EWCPKNSDGK YGGMMTMKDA LAGSVNTISA
     RLMNEVGPQP VIDLAEKLGV DVSNIPPVPS IALGTADLSL YEMVSAYSAF ANQGVYIEPQ
     IVSTIQDKNG TILYQHVPKT HDVISEEAAY VTLKLMEGVT QSGSGRRLRT GKSNRADYKN
     VVTGHPYSFT NPIAGKTGTT QNQSDGWFMG IVPNLVTGVW VGGDDRATHF RTTRYGQGAT
     MALPIWGLYM KDVYSNKDLK ISNGKFTKPE DISIEVDCEK YKSQNTDNDD YDELDF
//
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