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Database: UniProt
Entry: A0A285M9Y2_9FLAO
LinkDB: A0A285M9Y2_9FLAO
Original site: A0A285M9Y2_9FLAO 
ID   A0A285M9Y2_9FLAO        Unreviewed;       780 AA.
AC   A0A285M9Y2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN06265377_0065 {ECO:0000313|EMBL:SNY93959.1};
OS   Allomuricauda parva.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=1247520 {ECO:0000313|EMBL:SNY93959.1, ECO:0000313|Proteomes:UP000219048};
RN   [1] {ECO:0000313|Proteomes:UP000219048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25885 {ECO:0000313|Proteomes:UP000219048};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-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; OBEH01000001; SNY93959.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285M9Y2; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000219048; 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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR011815; PBP_1c.
DR   InterPro; IPR009647; PBP_C.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; TIGR02073; PBP_1c; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR   Pfam; PF06832; BiPBP_C; 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          55..216
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          294..553
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          683..769
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   780 AA;  89126 MW;  FF3BD102111F4E76 CRC64;
     MWKKHKFKLS LFLLLFLIWS FCLPKILFEE PTSTVVTSSD GILIGARIAD DGQWRFPQMD
     SIPERFKQSV LLFEDEYFYQ HLGFNPISIF NAIKHNLTKD TRRGGSTITQ QVIRLSRKNK
     SRTYFEKCIE LFLATRLEFR YSKDEILKLY ATHTPYGGNV VGLETASWRY FGIPAHELSW
     GQSATLAVLP NAPSLIFPGR NEQILLKKRN RLLKKLWDNK HIDQTTYELA ILEPLPKKPR
     PLPNSAPHLT ERIKKEHPGK RIKSSIDRHL QNQANILAER HYNQLKSNEI YNLSILVLDV
     ETRKVLSYVG NSPTIKAHGN YVDIITKKRS TGSTLKPFLF ASLLHEGQLL PNSLVKDIPT
     VINGYNPKNF NKKYAGAVPA SRALSRSLNV PAVRLLRQYG LQKFYNQLHK MNMRSLDRPA
     SHYGLPLILG GAEGSLWDIT KTYASAASTL NYFLSNSSTY RTNEFAEPSY LQESEIDFGE
     EQFESPILNA GALYHTFKSL QEVNRPEGDE NWQFFDSSQA IAWKTGTSFG FKDAWAVGVT
     PKYAIGIWIG NADGEGRPGL TGITAAAPLL FDVLDALPQS RWFQEPFDDL AELEVCKESG
     CIASTFCDII QKELLPIKGS RSKQCPYHHQ LFLDKEEAFR VNSDCYPLEN MIQKNWFGLP
     TVVEYYYANA HPNYKSLPPF LEGCHAEEKQ LMEFIYPKKN EEILLPRDLG KASREIIFKL
     AHQQQESTVH WYLDETYLGS TINFHELIVE NQLGNYTLTA VDDEGNRIQQ SLNVQMASEN
//
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