ID A0A2T5MEB8_9GAMM Unreviewed; 718 AA.
AC A0A2T5MEB8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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:PTU30925.1};
GN ORFNames=CJD38_11480 {ECO:0000313|EMBL:PTU30925.1};
OS Stenotrophobium rhamnosiphilum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Stenotrophobium.
OX NCBI_TaxID=2029166 {ECO:0000313|EMBL:PTU30925.1, ECO:0000313|Proteomes:UP000244248};
RN [1] {ECO:0000313|EMBL:PTU30925.1, ECO:0000313|Proteomes:UP000244248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GT1R17 {ECO:0000313|EMBL:PTU30925.1,
RC ECO:0000313|Proteomes:UP000244248};
RA Liu Q., Xin Y.-H.;
RT "Novel species isolated from glacier.";
RL Submitted (APR-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=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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:PTU30925.1}.
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DR EMBL; QANS01000004; PTU30925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5MEB8; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000244248; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000244248};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..217
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 304..544
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 628..703
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 718 AA; 77967 MW; 690217F54E9B4812 CRC64;
MALRKRFIAF GAVAVLLALG FTSWYLTAPP SPPDFAQVKK DYQPSDAWLL DRHGDVLAQV
RMEYGRRCVG WVPLDQISPA VIDPVRQAED HRFDTHGGVD GIALLGGLRD YALHRIRRGA
STITMQLAAK IDPELMAQRG RRGLKQKWRQ MRVAWQIESS WTKPQILEAY FNLVSFRSEW
LGVQTASTAM FGKSAAHLNR YEGAVLAALL RNPAANASVI AARACRIASE TNCQPYMQVA
TSALVRGLKP LMSETLAPHL ARALVHRGGE RVSSTVDLAT QNLVYAALAT QLSALSAAEV
RDAAAVVLDN ESGDVLAYVG SAGPSSTAWA VDGVNALRQA GSTLKPFLYS LAFEQRLLTP
ASLLDDSPVN LETGAGLYIP QNYDHEFRGH VSVRSALAGS LNVPAVRTLL LVGLEPFRDR
LHDIGYRNGL TESGEFYGFS LALGAPEVSL LEQANAYRTL ANAGRWSPVR LRAGDERATS
TQIISPESAY LVGSILSDNG ARAASFGLDS PLSTPFWSAV KTGTSKNMRD NWCIGYTTRY
TVAVWVGNFE GDPMHNVSGV TGAAPAWLEI ITALSRGSEP ASPKAPSGIV QSRITFHDHE
EPARNEWFID GTELSEIRAT PTGLGRAHIR APANGMIAAL DPDIPVAHQN VLFEAEGADN
ARWVLDGRDI GMASKKQLWV PRPGRHRLQV LSKDGKEVDA VSFEVRATVS EKRGPINR
//
