ID I3CCV3_9GAMM Unreviewed; 745 AA.
AC I3CCV3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BegalDRAFT_0528 {ECO:0000313|EMBL:EIJ41446.1};
OS Beggiatoa alba B18LD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ41446.1, ECO:0000313|Proteomes:UP000005744};
RN [1] {ECO:0000313|EMBL:EIJ41446.1, ECO:0000313|Proteomes:UP000005744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18LD {ECO:0000313|EMBL:EIJ41446.1,
RC ECO:0000313|Proteomes:UP000005744};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA Mueller J., Woyke T.;
RT "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL Submitted (NOV-2011) 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}.
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DR EMBL; JH600070; EIJ41446.1; -; Genomic_DNA.
DR RefSeq; WP_002683401.1; NZ_JH600070.1.
DR AlphaFoldDB; I3CCV3; -.
DR STRING; 395493.BegalDRAFT_0528; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_1_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005744; 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; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
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 ECO:0000313|EMBL:EIJ41446.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000005744}.
FT DOMAIN 72..237
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 321..556
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 651..720
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 745 AA; 83827 MW; 71D6520CB8C5BCCB CRC64;
MMLRQYLSAF FAKRTVRILF ILLILLAIGI TWQTRQEIQP FPPTLSLANT DVRKVQLLDK
NGIPLIITYQ NDWNLHNIVP LHKIPKTLQQ IFILSEDKRF YEHHGVDWSA RWHAIAQNIK
SFRIVRGAST MTEQVVRMLH PRPRTFWSRW VESFEAAHLE EQYSKADILE FYLNQIPYAS
QRRGVVQAAR HYFDRDLDTL NLKEMMALSV LVRSPSRLDL RRGTTEIERP LKVLAQRLLE
QGVINETEYQ TALNTPLELR EPPLPVQAAH FVQYVYTSQA VDKLQTRGHL YTTIDAKVQT
AVQAILDQRL SDLQKQKVSN GAVLIIDNQD ASVVAWVNSG ISSPNIPVSF IDTVTTPRQP
GSTLKPLLYA MALAKGWTAA TLIDDSPLAE SVGTGLHNYR NYSRSHYGQL RLRDALGNSL
NIPAIRTIQF VGATQFLRQL QELGMQSLTA TADFYGDGLA LGNGAVTLYE LVQAYTTLAN
NGVFRPLHVL RNQDTGIQRA IFTPEVSQII GNILSDSDAR RLEFGRGALL RFPVQTAVKT
GTSTDYRDAW AVGFNYRYTV GVWFGNLTEE PMSEVSGSTG PALALRAVFA ELNRYTETQP
LPLSPRLVKM DICRESGLQA SGNCPSRTEW FVAGTEPNQA LPQLLNMAMV ESIRLQQPND
GLQLALDPRI PDDKEAFAFA LANPLPNAGT QIDWLVNGQI IGTTPATNPR FLWQVQRGTH
IAQARLWTET SEQPLETPAV MFYVK
//
