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Database: UniProt
Entry: A0A1H9CTF3_9BACT
LinkDB: A0A1H9CTF3_9BACT
Original site: A0A1H9CTF3_9BACT 
ID   A0A1H9CTF3_9BACT        Unreviewed;       761 AA.
AC   A0A1H9CTF3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-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=SAMN05444359_10511 {ECO:0000313|EMBL:SEQ04500.1};
OS   Neolewinella agarilytica.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC   Neolewinella.
OX   NCBI_TaxID=478744 {ECO:0000313|EMBL:SEQ04500.1, ECO:0000313|Proteomes:UP000199021};
RN   [1] {ECO:0000313|Proteomes:UP000199021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24740 {ECO:0000313|Proteomes:UP000199021};
RA   Varghese N., Submissions S.;
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=2.4.1.129;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988};
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DR   EMBL; FOFB01000005; SEQ04500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9CTF3; -.
DR   STRING; 478744.SAMN05444359_10511; -.
DR   InParanoid; A0A1H9CTF3; -.
DR   Proteomes; UP000199021; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199021}.
FT   DOMAIN          33..195
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          273..404
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          671..757
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   761 AA;  83922 MW;  78D9D31D8660E4CB CRC64;
     MPRPLFDAPL STQLLSAEGE LLSARIAADG QWRMPAADSV SSRLKAAVLV YEDRRFRQHW
     GVSLSGIGRA IRDNWQAGAV VSGGSTITMQ VARMARGNKS RTLGQKVMEA LWATRMEWRY
     DKDEILAFWL ANAPFGGNVV GAEAAARRYY GRSPEELSWA EAATLAVLPN SPALIHPGRA
     RDALRDKRDR LLDQLAAAGH CSSEEVGLAR LEPLPERPHP LPREAGHLLE RLRSDKGAGR
     YRSSLNAALQ RRVAGMVREH HLALAGNGIH NAAAMVTEVS SGRVVAYVGN VPDLAPAFAP
     DVDVITSPRS PGSLLKPMLY ALAQEEGRIS SKQLLPDVPT SFGDFRPANF YRDYDGAVPA
     DEALARSLNI PFVYLLQDYG TERFHAALRE YGFKQLLRGP DHYGLSLVLG GGEITMEEIN
     AWFLGMARQQ RYFYERQGWY AEADFQPATL LDAESRDPLA DLNQVAGAVG AGAGFKTLEA
     LTALNRPDET GASHRFSSHQ KVAWKTGTSF GFRDAWAVGC TPAYVVSVWT GNADGEGRAG
     LVGVRAAAPL LFRILRALEQ DGGEAPRWFE APYDDMTEAT VCQTSGYLAG PDCPTTAEWQ
     AANAERASVC RFHQRIFTTP EGDYRVNQDC APGQLVTGRQ FQLPSRQAYF YRRRHPEYRS
     LIPWHPDCAN AADAGSPMQF IYPHGNGAIS AGKNWHGEIE PVFFELSHQK EESTVHWHID
     GEFMGSTTRF HSLAVEITEG RHTITVVDED GARLERRFVV R
//
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