ID A0A399JC32_9RHOB Unreviewed; 686 AA.
AC A0A399JC32;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:RII40196.1};
GN ORFNames=DL237_02425 {ECO:0000313|EMBL:RII40196.1};
OS Pseudooceanicola sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=2211117 {ECO:0000313|EMBL:RII40196.1, ECO:0000313|Proteomes:UP000265848};
RN [1] {ECO:0000313|EMBL:RII40196.1, ECO:0000313|Proteomes:UP000265848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CY03 {ECO:0000313|EMBL:RII40196.1,
RC ECO:0000313|Proteomes:UP000265848};
RA Zhang Y.-J.;
RT "Pseudooceanicola sediminis CY03 in the family Rhodobacteracea.";
RL Submitted (AUG-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:RII40196.1}.
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DR EMBL; QWJJ01000002; RII40196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399JC32; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000265848; Unassembled WGS sequence.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..686
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017399125"
FT DOMAIN 80..233
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 310..519
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 605..682
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 686 AA; 73321 MW; 0D6D1162CFB7A2F3 CRC64;
MTRDRTRRDW RGTLVALSVA ALLALAAGRD AADTWIDATV LPPLHPATAV EMRAADGSLL
SAYMVDDGRW RLAMSGPADP LYLRMLVAYE DRRFATHHGV DPRAMARALW QMLTNGHVVS
GGSTLTMQVA RLLEKGSTGR WSGKLRQTRV ALALERTLSK DQILDLYLTL APMGGNIEGL
RAATLAWFGK EPTRLTPAEA ALLVALPQSP EARRPDRAPL VAQAARDRVL TRMAQDGVIS
TDTARAAKTD RIPTQRRRFP ALAPHLTDRA LAAHPDLARQ TLTIEAPLQA ALESLAATAL
EGRKSQLSLA ILVADHRDGR ILASVGSRGF SDTGQGFVDM TQALRSPGST LKPLIYALAF
DQGLAHPETL IDDRATDFNG YQPTNFDGTF RGPVRATDAL QLSLNLPAVL LTEALGPANI
MAALRRGGLD PHVPGGQAGL AIALGGLGLS LQDLVQLYAG LANDGHAHPL YWQAEAAVQQ
PLRITASASA WQVSHILSGL APPAGAPLNR LAYKTGTSYG HRDAWAIGFD GAHVIGVWVG
RPDGTPVPGV FGGDTAAPVL FEAFQRLKPT LTPLPPPPPE TLLVEGSKLP LPLREFHRRS
IGLSVERDAP ELVFPPDGVA LDAMPEGLPV RVRQGKPPFT WLVNGTPVVI GSRRSDAILS
AMGLGFSEVT VVDANGRSDR ANVRLQ
//