ID D4GK62_PANAM Unreviewed; 775 AA.
AC D4GK62;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 18-JUN-2025, entry version 76.
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:ADD78030.1};
GN OrderedLocusNames=PANA_2863 {ECO:0000313|EMBL:ADD78030.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD78030.1, ECO:0000313|Proteomes:UP000001702};
RN [1] {ECO:0000313|EMBL:ADD78030.1, ECO:0000313|Proteomes:UP000001702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD78030.1,
RC ECO:0000313|Proteomes:UP000001702};
RX PubMed=20348253; DOI=10.1128/JB.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
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; CP001875; ADD78030.1; -; Genomic_DNA.
DR RefSeq; WP_013026738.1; NC_013956.2.
DR AlphaFoldDB; D4GK62; -.
DR STRING; 706191.PANA_2863; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; pam:PANA_2863; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001702; 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:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR FunFam; 1.10.3810.10:FF:000006; Penicillin-binding protein 1C; 1.
DR FunFam; 3.40.710.10:FF:000021; Penicillin-binding protein 1C; 1.
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 NCBIfam; NF008414; PRK11240.1; 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:UP000001702};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 60..226
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 302..559
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 688..772
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 775 AA; 85451 MW; 1D469DB30BC19023 CRC64;
MIKNRHIKKR WVALPLFILA LLLIPLILDR LFPLPLKEVQ PARVVVAEDG TPLWRFADDQ
GIWRYPVTPA DVSPTYIQAL LTYEDRWFWY HPGINPLALL RAAWQDLRHG SVISGGSTLT
MQVARIIDPQ PRTLRGKLIQ AWRALQLEWH LSKYDILTLY LNRAPFGGTL EGIGAASWSW
LGKAPSQMTR GEAALMAVLP QAPSRLRPDR WPERAEAARN KVLDRLAQYH VWSPRRVAEI
RQEPVWLPPR QMPQMAPLLA RRLLSMTTHD KIVSTLDLSL QRELESMALN VKNQLPPRTS
LAILVVDHTT MAVRGYVGSA DFGDDSRFGH VDMIASVRSP GSVLKPFVYG MALDEGLIHA
ESLLQDVPRR FGDYRPGNFD TGFHGPVSAS EALVRSLNLP AVQLLEALGP KNVAARLRNV
GLNLRFPPGT EPNLSLILGG TGARMDDIVA AYSAFARHGN AGQLRWMADQ PLQERPLLSP
GAAWIIRRIL GGEAQPAGNG SAPAVVPLAW KTGTSYGYRD AWAVGINPRY LIGVWVGRPD
ATPVAGQFGF ASAVPVMNQV NNVLMNRLAG RAVPTEPRPA SVSVAGICWP GGQPLPEGDE
NCRQRRQSWV LNDTLPPTLL APGQESLSGL HLHYWQNEQG LRVAADCPHA ISHERLVWPL
PLEAWLPPQE RRAQRLPAVD PRCPPLQQGS SAPLIVTGVI DGQRVQPLPG NTTLVIPVAV
QGGQGVQRWW FLNGEPLETQ SQNGTLSLPL DRAGDYQLVV MDEAGQLASV VFTRG
//
