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Database: UniProt
Entry: A0A399JC32_9RHOB
LinkDB: A0A399JC32_9RHOB
Original site: A0A399JC32_9RHOB 
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
//
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