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Database: UniProt
Entry: A0A2D0HBZ2_9NOSO
LinkDB: A0A2D0HBZ2_9NOSO
Original site: A0A2D0HBZ2_9NOSO 
ID   A0A2D0HBZ2_9NOSO        Unreviewed;       772 AA.
AC   A0A2D0HBZ2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   Name=pbpC {ECO:0000313|EMBL:PHM07045.1};
GN   ORFNames=CK516_29545 {ECO:0000313|EMBL:PHM07045.1};
OS   Nostoc sp. 'Peltigera malacea cyanobiont' DB3992.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1206980 {ECO:0000313|EMBL:PHM07045.1, ECO:0000313|Proteomes:UP000223928};
RN   [1] {ECO:0000313|EMBL:PHM07045.1, ECO:0000313|Proteomes:UP000223928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DB3992 {ECO:0000313|EMBL:PHM07045.1};
RA   Gagunashvili A.N., Andresson O.S.;
RT   "Distinctive characters of Nostoc genomes in cyanolichens.";
RL   Submitted (AUG-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   -!- 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:PHM07045.1}.
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DR   EMBL; NSHF01000387; PHM07045.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0HBZ2; -.
DR   Proteomes; UP000223928; 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:UP000223928}.
FT   DOMAIN          60..232
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          325..597
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          667..752
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   772 AA;  86191 MW;  C60CD2D9C1A95730 CRC64;
     MKLILRSLLK LKRTSKVILA VLLICLVVRL LPYFAPIRAA DIAQNHLAMQ FSDRNGLPLG
     TLLTRDQEHT SVVPLNQVSP HFIHAILAAE DGSFYHHGAL DMKAIIRASK EAIHAKRIVS
     GASTITMQLA RMLDPVPRSF SGKLSEIWLS WRLTAGMNKD EILSAYINRL PMGGNIYGVE
     AAAQIYFSIP ASELNLAQAS LLAAIPNNPT YFNPYEHWER LKQRQKYVLN RMVQEKYING
     AMATPTSATN ATRTQTEKVV FQSRQRGIIA APHFLFWLAN QFDKRQTEQN SPIRTTINRP
     LQQFVEAQVQ QVISSLAANN VHDAAALVID NQTGEVLAYV GSPDYFNEAK LGRNDGVQAL
     RQPGSTLKPF VYELALEKGL IRPNTILADV PARYAIPGAK LYSPTDYTER FLGPVRVRIA
     LANSLNVPAI KVLEKVGVET FLKRLHQLGF EHLNQTPEHY GLGLTLGSGE VSLWELARAY
     LTIARQGDAT PIVSTFSNSP IQNPKYTIQN STTIWQLITN ILSDSYARAT AFGVDSVLNL
     PFPVAVKTGT SSNFRDTWTV GFTTDYTVAT WVGNFNGEPM RQVSGVTGAA PLWNRIMLHL
     HEHQEPTGFP SPEGLVQLPV CAISGLRPTP DCTSVVQEYF YPEDKSNYER DNQFNLPPEY
     DEWLAKQQQS NFTSANLRIL SPHHGDLFLL YPGEKAKQKL EFKLAGNKSA PVEWWLNGEK
     LDTNSANSLF WNLRPGKWTL EARSGEMSDK VSFQVELANI KPTRRGFSIS NN
//
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