ID B0VIB0_CLOAI Unreviewed; 682 AA.
AC B0VIB0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=mrcA {ECO:0000313|EMBL:CAO81098.1};
GN OrderedLocusNames=CLOAM1238 {ECO:0000313|EMBL:CAO81098.1};
OS Cloacimonas acidaminovorans (strain Evry).
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO81098.1, ECO:0000313|Proteomes:UP000002019};
RN [1] {ECO:0000313|EMBL:CAO81098.1, ECO:0000313|Proteomes:UP000002019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Evry {ECO:0000313|Proteomes:UP000002019};
RX PubMed=18245282; DOI=10.1128/JB.01248-07;
RA Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA Weissenbach J., Le Paslier D.;
RT "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT provides a first glimpse of a new bacterial division.";
RL J. Bacteriol. 190:2572-2579(2008).
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}.
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DR EMBL; CU466930; CAO81098.1; -; Genomic_DNA.
DR RefSeq; WP_015424956.1; NC_020449.1.
DR AlphaFoldDB; B0VIB0; -.
DR STRING; 459349.CLOAM1238; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; caci:CLOAM1238; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_4_0; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000002019; Chromosome.
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: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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000313|EMBL:CAO81098.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAO81098.1};
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:UP000002019};
KW Transferase {ECO:0000313|EMBL:CAO81098.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..234
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 342..578
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 682 AA; 77655 MW; F12D06E673291503 CRC64;
MKASTKEKLY SVLKYLWFAF CFITGIFVGA LWFYHDSLPP TSELRNYTLR SGSEVYDRNG
KMVYLFAFEK RKLVSLKELP QYLIDALIIT EDKHFYHHFG IDILGNIRAL AVDIVRLDFS
QGASTITQQM ARNMFLTLDK RLSRKLKEII LALRIEREFT KDEILEIYFN KIFWGGQIHG
VETASLYYFG KHARDLTLAE SAALVGMIQR PNYYNPAKHP ERLIERRNMI LGKMLKAKKI
TQEEYNEAVA SKITGDRSSL QQYSTDYYIE HIRLYLERKY GTEKLFEGGL KIYTPMDVDL
SVYADSVLNR YLSNVEKGYP ASMRYDSVPK NSVDINTRYL QGGILLMENS TGQVLAMLGG
RNFTHSKFNR ITQAKRQPGS AIKPTYYTAA IEKGYTPATV INDAPITLTG GNGKDWTPQN
FSRKYYGPSR MRTAITYSYN VWAVKTVMDL GLDVVNDAFR RFGIDAKAED YSAALGAYEV
TPINLISAFT TFPNNGFRTK PVFITKVEDV NGKVLERSST AKYDVTTPQV AFIMTSLLQS
VVTSGTGAAA RNNYYWQAAG KTGTSSDHRD AWFIGFNRKY TLGIWNGFDN NAAISASASC
APIWGQIMTK AIRNENKGRL PKSDDPRYSF VVPDKIVKRT INPKTGFVSE YGIEEYFIED
NIPPARSDTL SYNYYPTRWE NP
//
