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Database: UniProt
Entry: A0A558RAD4_9SPHN
LinkDB: A0A558RAD4_9SPHN
Original site: A0A558RAD4_9SPHN 
ID   A0A558RAD4_9SPHN        Unreviewed;       706 AA.
AC   A0A558RAD4;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, 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   Name=pbpC {ECO:0000313|EMBL:TVV76353.1};
GN   ORFNames=FOY91_04530 {ECO:0000313|EMBL:TVV76353.1};
OS   Sphingomonas solaris.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Sphingomonadales; Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2529389 {ECO:0000313|EMBL:TVV76353.1, ECO:0000313|Proteomes:UP000318681};
RN   [1] {ECO:0000313|EMBL:TVV76353.1, ECO:0000313|Proteomes:UP000318681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R4DWN {ECO:0000313|EMBL:TVV76353.1,
RC   ECO:0000313|Proteomes:UP000318681};
RA   Tanner K., Pascual J., Mancuso C., Pereto J., Khalil A., Vilanova C.;
RT   "Sphingomonas solaris sp. nov., isolated from a solar panel from Boston,
RT   Massachusetts.";
RL   Submitted (JUL-2019) 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}.
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:TVV76353.1}.
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DR   EMBL; VNIM01000011; TVV76353.1; -; Genomic_DNA.
DR   RefSeq; WP_145148672.1; NZ_VNIM01000011.1.
DR   AlphaFoldDB; A0A558RAD4; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000318681; 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:UniProtKB-UniPathway.
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:UP000318681};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          68..216
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          303..570
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          620..701
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   706 AA;  74739 MW;  8351F98FF52C79F5 CRC64;
     MPSRLARHLL VAFALLGLGG LAWLWIATRP PAVPGFAAAR AAWRPSEAWL YDRDGRLLDS
     ERVDFSVRRL GWTPLAATAP TLRKAVVLAE DHRFYAHDGV DWLATASALR TRVAGGRSRG
     ASTITMQLAG FLGGDLARPG ARGWRDKLRQ MRAAWAIEAG WTKPQILEAY LNLAGFRGEA
     QGVAAAAQTA FAKPPAALSR NEALLLVALL PDPRADAATV ARRACRLRGA GACDDLVAGA
     EGMLASGRRL ALDPGLASHL AGRLLRRPGM RVRTMIDRTV QQAATTALRR QLLGLGATRA
     RDGAVVVVEN ATGAVLAYVG GVGGAATAAA VDGANAYRQA GSTLKPFLYG LAMEHGWLPP
     ASILDDAPVQ LDTASGLYVP QNYDRTFRGA VSARSALAGS LNVPAVRTLI LTGVEPFRDR
     LWDAGYRGLT EDGAYYGFSL ALGSAEVTLL EQANAYRTLA NGGRFTPLRL TAGAPVQPAR
     PVFTPQAAWL AADMMADPGA RAATFGLESA LRLPFWAAVK TGTSKAMRDN WCIGFTDRFT
     VAVWVGNLEG DSMRAVSGTS GAAPVWREVM LALHRHRPGL PPPRPPGIEA RRVAFAGEIE
     PTRREWFLAG TGQAALAAAP PGARRPRITA PVSGSVYALD PDIPLPRQRL RIAVAGGAAG
     HRLLLDGRDL GAASASPLIL AGPGPHWLVL TDTGGRAVDR VLFTMR
//
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