ID A0A2N7WFX8_9BURK Unreviewed; 756 AA.
AC A0A2N7WFX8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 18-JUN-2025, entry version 28.
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:PMS28264.1};
GN ORFNames=C0Z19_00595 {ECO:0000313|EMBL:PMS28264.1};
OS Trinickia soli.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Burkholderiaceae; Trinickia.
OX NCBI_TaxID=380675 {ECO:0000313|EMBL:PMS28264.1, ECO:0000313|Proteomes:UP000235347};
RN [1] {ECO:0000313|EMBL:PMS28264.1, ECO:0000313|Proteomes:UP000235347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP25-8 {ECO:0000313|EMBL:PMS28264.1,
RC ECO:0000313|Proteomes:UP000235347};
RA Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
RL Submitted (JAN-2018) 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:PMS28264.1}.
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DR EMBL; PNYB01000001; PMS28264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7WFX8; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000235347; 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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000235347};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..756
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014951220"
FT DOMAIN 51..217
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 315..555
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 652..734
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 756 AA; 80979 MW; A30B3624E7EDD2DC CRC64;
MQTTLRAASV RATFCALMLL AAPCVQALPT FDQVRTQWRS SDWLLLARDG EPLQRTRVDL
KERRGDWVSL ADVSPALREA IVVSEDKRFY EHSGVDWRGA AAAAWANLWN TRTRGASTVT
MQLTGLLSDD PQHSGQRSIA QKAGQAVSAL WLERSWRKDQ ILEAYLNLVP FRGEAVGLSA
LSLTLFGKAP SGLDEREAAV AAALIRSPNA SYPIVSARAC RILRDLKAPR RCDNLASYVQ
LAFARPPPAV LSVAPEAEML APHFARRVAG EVHPTAGMRI VTTLDAKLQR FATATLRRTL
VELNAPAHAR NVHDGAIVVL DNATGNVLAW VGSSGSLSQA GEVDAVLARR QAGSTLKPFL
YGQAIDEHRL TTASLLDDAP LDLAAGGGLY IPQNYDKDFK GWVSVRTALG SSLNVPAVRT
LVMVTPHRFA MTLKALGLPL AESGDYYGYS LALGSADITL LSLTNAYRAL ANGGVASATH
DLPQAKTTRD VRVQNASRRV LSADAAYIIT TVLWDNNART RTFGFDSPLA TRFFSAVKTG
TSKDMRDNWT IGFTSRYTVG VWVGNADGSA MWDVSGVTGA SPIWAAVVGY LHRHVSSLPP
AMPAGVVKTR VSFDGNVEPS RNEWFLKGSE LTTVGLAADA GNASLPGAMR GARSGASRIG
SPTDGTLFAL DPDIPAARQR IVFERVSGSS TGSVWRLDGK PLGHAQRLPW PPWPGRHLLE
LVNAQGASVD AVHFEVRGAT ARAAGASKAG GTLPPR
//
