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Database: UniProt
Entry: A0A2V4AFM2_9BACT
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Original site: A0A2V4AFM2_9BACT 
ID   A0A2V4AFM2_9BACT        Unreviewed;       799 AA.
AC   A0A2V4AFM2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=DF185_02020 {ECO:0000313|EMBL:PXY02894.1};
OS   Marinifilum breve.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae.
OX   NCBI_TaxID=2184082 {ECO:0000313|EMBL:PXY02894.1, ECO:0000313|Proteomes:UP000248079};
RN   [1] {ECO:0000313|EMBL:PXY02894.1, ECO:0000313|Proteomes:UP000248079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC075 {ECO:0000313|EMBL:PXY02894.1,
RC   ECO:0000313|Proteomes:UP000248079};
RA   Fu T.;
RT   "Marinifilum breve JC075T sp. nov., a marine bacterium isolated from Yongle
RT   Blue Hole in the South China Sea.";
RL   Submitted (MAY-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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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:PXY02894.1}.
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DR   EMBL; QFLI01000001; PXY02894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V4AFM2; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000248079; 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: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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          85..264
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          438..687
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   799 AA;  90719 MW;  07718B697637CADB CRC64;
     MAKTKKTTSR KTNSKRKTSS KKKTKKRSIK SYIIRLGLLA IACALVGIGL LFSTVYLGFW
     GKLPDYYTLR NIKNADASEI YSEDGAILGR VYAENRTNVN FKDISPNVIN SLIATEDVRF
     YEHQGVDQRS MLRVLVKSLI MRDRSSGGGS TLSQQLAKNL YPRKRYGAIS MPINKIREAI
     TASRLEKIYS KKEILQLYLN TVSFGENVFG IESASRQFFS KPASALKTQE CAVLIGMLKA
     PTYYNPRLHP DRSKQRRNVV LNQMAKYEYI SETKAKQLKA LPLGLRYNNQ ASKNGLAPYL
     RENIRIQTNK ILADYPKEDG SYYDIYRDGL KITTTLDSKL QAYAEQSVGE HLKRLQDLFY
     KHWGTSKPWD NKKDILSDAK RRSDRYKKLK KSGKSEQEIN KIFNKKVDMK IFTWSGEKNV
     NMSPNDSIKH YVQLLNTGFL AMEPHSGKIK AWVGGIDFNH FKYDHVTAKR QVGSVFKPVV
     FSAALEEGVS PFEYLPNERK VYEEYDNWSP RNADNKYEGS YSMEGALAES VNTIAVDVLL
     QTGIRDAIVL AEEMGVDSNL PKVPSLALGT ANISLFEMIQ VYATLANRGV HVDPYYLVKI
     EDKNGNLIAD LSKQRGENRF VLSPQNADII NHMLQAVVNS GTGKSLRNVY KLEGDLAGKT
     GTTNSHADGW YIGYNSNLVA GAWVGADDMR VHFRSLTLGQ GASMALPIYG KFMHKLSRNR
     KFTNYSYASI HKPDNDILAQ LSIPHYMPKD SGLLKNIFGV KAKDRDKLME RKQRKEKRKA
     KRKSIYQRIK NIFKKKNKD
//
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