ID A0A366E7G6_9BACI Unreviewed; 722 AA.
AC A0A366E7G6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DES48_10597 {ECO:0000313|EMBL:RBO98247.1};
OS Paraliobacillus ryukyuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Paraliobacillus.
OX NCBI_TaxID=200904 {ECO:0000313|EMBL:RBO98247.1, ECO:0000313|Proteomes:UP000252254};
RN [1] {ECO:0000313|EMBL:RBO98247.1, ECO:0000313|Proteomes:UP000252254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15140 {ECO:0000313|EMBL:RBO98247.1,
RC ECO:0000313|Proteomes:UP000252254};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-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 -!- 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:RBO98247.1}.
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DR EMBL; QNRI01000005; RBO98247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366E7G6; -.
DR STRING; 200904.GCA_900168775_01205; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000252254; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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:SF36; PENICILLIN-BINDING PROTEIN 1F; 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 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:UP000252254};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..237
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 330..600
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 722 AA; 80478 MW; 2B4EF5536B00FF9A CRC64;
MKYIDRMRQI RWSSWVKWLS IGFGSMALLA IVGFMIIIYG GGLVVDEEDL ILPATTTVKT
QDGDVVGKLY QENRNLVTID QVPKHVQQAF VAVEDVRFYD HAGVDFNAVA RAVYKDVVAL
QKVEGASTIT QQLAKNLFLH DEKTWMRKTK EVMASIYLER HYSKDKILEL YMNEVYFAHG
IYGIGTAADY YFDKPVEELT ITEGAMLAGL VKAPNTYSPY LDKDATKKRR DIVLSQMEKA
GMLETEEKLT LQGKTVDVVE QKEAQSPWLD DYLDVVIREA ASQYQLTTEE LKRGGYDITV
YMNNVAQKTA YQQLQQENFY YGSEPNVESS FVLMNQKSGA LEAVIAGRNF QIGEHNRAML
RRQPGSVLKP LAVYGPALMN NYQPYSLLQD RAQSYDDYQV ANADGGYAGE ISMYQAIAES
KNATAVWLLD QIGIDYSKTY LEKMDISLSD QGLAIALGGL KNGLTPIEIA AGYRTFIHDG
EWIQPHAIVS IHDRNGTLIG EANPTTTQVF SKQVAWSMLR MLENVVNNGT ATAGEYAKAL
AGKTGTTQHP QVEGQAKDAW FAGVTPEYTT ALWMGYDQSD ETHYLTKGSS AATIATKAIL
QAIDQQQPLG DQFTKPINVD DVEQPIQLPV IDDLDVSYQL GGWSLVQGKL TWTASDDERV
VYHIYSVTDA GSKKIGQVQG KGQFILTDVS VFQSSSYYVV PYNQLTKQQG TKSNQITLSF
GN
//
