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Database: UniProt
Entry: A0A1I7HJ14_9FLAO
LinkDB: A0A1I7HJ14_9FLAO
Original site: A0A1I7HJ14_9FLAO 
ID   A0A1I7HJ14_9FLAO        Unreviewed;       786 AA.
AC   A0A1I7HJ14;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   18-JUN-2025, entry version 26.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE            EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN   ORFNames=SAMN05216480_109137 {ECO:0000313|EMBL:SFU60750.1};
OS   Pustulibacterium marinum.
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Pustulibacterium.
OX   NCBI_TaxID=1224947 {ECO:0000313|EMBL:SFU60750.1, ECO:0000313|Proteomes:UP000199138};
RN   [1] {ECO:0000313|EMBL:SFU60750.1, ECO:0000313|Proteomes:UP000199138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12333 {ECO:0000313|EMBL:SFU60750.1,
RC   ECO:0000313|Proteomes:UP000199138};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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=2.4.99.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00049902};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR   EMBL; FPBK01000009; SFU60750.1; -; Genomic_DNA.
DR   RefSeq; WP_394331590.1; NZ_FPBK01000009.1.
DR   AlphaFoldDB; A0A1I7HJ14; -.
DR   STRING; 1224947.SAMN05216480_109137; -.
DR   Proteomes; UP000199138; Unassembled WGS sequence.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:InterPro.
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; IPR050396; Glycosyltr_51/Transpeptidase.
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   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199138};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          62..226
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          305..564
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          693..779
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   786 AA;  88349 MW;  DF9BCE52582C5B8E CRC64;
     MSMAPLSTKA FVKRNRIKLI GLTLLLIAYY CCLPQPLFTT PTATVIESSD GTLLGAKIAS
     DGQWRFPKMD TVPEKFKQCI VQFEDAYFYQ HPGINPVSMG KALVSNIKAG KTVRGGSTLT
     QQVIRLSRKG TSRTYLEKLW ESTLATRLEF RYSKDEILNF YASYAPFGGN VVGLDMASWR
     YFGVLPQQLS WAESATLAVL PNAPSIIYPG KNQETLHQKR DQLLLKLKNE GIIDDTTYQL
     ALAEDLPQQA FPIPRTASHL TEYIAKKHKG ERLQTTIDQK LQHQVNTLVA QHHRKLKQNH
     VYNASVLVLD VATRNVLAYV GNAPTDNAHE KDVDMMHAPR STGSVLKPLL YAAMLDNGEL
     LPQMLIPDVP TEIAGYQPEN FDESYSGAVP ADEALARSLN IPAVRLLQRH GLEKFRDELD
     AFHLKNINKP ANHYGLTLIL GGAESNLWDL CKTYASLAAT LNHFNETSSE YYTDEFQEPN
     VYASQKKDFG SKSTQKTVFN AGSIYSVFEA MKQVNRPDSE VSWEYFDSSR EIAWKTGTSF
     GNKDAWAIGV NKKYVVGVWV GNADGEGRPQ ITGTSSAAPL LFDVFNVLPK SSWFEMPYDE
     MMEVRVCAQS GYLASDICPA KTQWVPKAGA HANLCHYHHT IHVDTQHQFR VNSSCETVDQ
     IAHVSWFTLP PLMEFFYKKT HANYKTLPPF RTDCTTSEEK MMEFIYPKDY STITLAKDFD
     GKINELVVKV AHRKPATTLL WYLDDSFLKQ TTQFHEVSIN PPTGQHLITV TDIDGNTIAS
     HIIINK
//
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