GenomeNet

Database: UniProt
Entry: A0A2D1U4D2_9SPHI
LinkDB: A0A2D1U4D2_9SPHI
Original site: A0A2D1U4D2_9SPHI 
ID   A0A2D1U4D2_9SPHI        Unreviewed;       786 AA.
AC   A0A2D1U4D2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   18-JUN-2025, entry version 29.
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:ATP56394.1};
GN   ORFNames=CPT03_07865 {ECO:0000313|EMBL:ATP56394.1};
OS   Pedobacter ginsengisoli.
OC   Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC   Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=363852 {ECO:0000313|EMBL:ATP56394.1, ECO:0000313|Proteomes:UP000223749};
RN   [1] {ECO:0000313|EMBL:ATP56394.1, ECO:0000313|Proteomes:UP000223749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T01R-27 {ECO:0000313|EMBL:ATP56394.1,
RC   ECO:0000313|Proteomes:UP000223749};
RA   Weon H.-Y., Lee S.A., Sang M.K., Song J.;
RT   "Whole genome of Pedobacter ginsengisoli T01R-27 isolated from tomato
RT   rhizosphere.";
RL   Submitted (OCT-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=2.4.99.28;
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP024091; ATP56394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D1U4D2; -.
DR   KEGG; pgs:CPT03_07865; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000223749; Chromosome.
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:UP000223749};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          51..210
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          293..573
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          695..771
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   786 AA;  88616 MW;  174299EF035BAA2F CRC64;
     MTDVVFLILL LIFLFSLPSK LFVSPTSYVV EASNGDLLSA SIAKDGQWRF PVADNIPEKF
     AQCLVAFEDK RFYYHPGVDP IAMARAMRQN FKAKSVISGG STISMQVIRL SRRESRTVWQ
     KLIEIILAIR LEASYSKKEI LKLYAGNAPF GSNVVGLDAA AWRYFGRSAE SLSWGEMATL
     AVLPNSPSLV HPGKNSPRLI KKRNDLLDKL AVLKIIDQST ANLSKLEPIP GKPQQLPQNA
     PHLLNRFKAE RSALKTGSTR ITSTLDYDLQ LRVSSLLKRY NNRYRANDIN NIAALVLDVK
     KGTVLSYVGN IYQPENTELE SHVDMIKAPR SPGSTLKPIL YASMLNDGFI LPKTLIADIP
     TQIGGYSPQN YDMGYDGAIQ ADRALSRSLN IPAVKMLQNY KYQRFYDKLK QLGFTTLNKP
     ADHYGLSLIL GGSEVTMWDL ARTYMGMART LNHFNDYKGR YNPHDYDEPL YVNEQRDKRF
     DEFETEVNSA IDHGSIWNAF NAMEELMRPG EEGLWEQFSS SQRLAWKTGT SFGFRDAWAV
     GLNPNYVVCV WVGNADGEGR PGLTGIDAAA PVMFDIFKQL PVVKWFKTPT SKLKKIVVCK
     ESGYKAGEYC TDKVIQLVSP AGEKTGLCPY HKMVHLDRTG TYRVTDECEA PSAMVHKSWF
     ILPPSMEYYY KIKNSDYKEL PPFKPGCGDA GNNFVMEMIY PRNYATVYIP VEFDGTRGKI
     VLNATHRNAN AKIYWHIDNE YVATTKNYHQ LAVSPAPGKH ILTLVDENGE RLVQHFTVLE
     KEKEKN
//
DBGET integrated database retrieval system