ID H0QIS5_ARTGO Unreviewed; 730 AA.
AC H0QIS5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ARGLB_027_00550 {ECO:0000313|EMBL:GAB12726.1};
OS Arthrobacter globiformis NBRC 12137.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB12726.1, ECO:0000313|Proteomes:UP000003828};
RN [1] {ECO:0000313|EMBL:GAB12726.1, ECO:0000313|Proteomes:UP000003828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB12726.1,
RC ECO:0000313|Proteomes:UP000003828};
RA Miyazawa S., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Arthrobacter globiformis NBRC 12137.";
RL Submitted (DEC-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 -!- 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:GAB12726.1}.
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DR EMBL; BAEG01000027; GAB12726.1; -; Genomic_DNA.
DR AlphaFoldDB; H0QIS5; -.
DR STRING; 1077972.ARGLB_027_00550; -.
DR eggNOG; COG0744; Bacteria.
DR Proteomes; UP000003828; 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: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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000003828}.
FT DOMAIN 66..254
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 355..638
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 703..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 78400 MW; DA6C648B768E2F5F CRC64;
MALALAKLLG FVIVSCLCGV LVASFLVPGA ALAGTSVSRS ISYFNSLPTE LAVPAPSQTT
RMLTADGKLI ATFYSENRVR VPLKQMSPFI RKAVVAIEDS RFYEHSGVDT QGILRALTSN
LTRGDRQGAS TLTQQYVTNI VNESLISEGR EDQVVLSGQK TMGDKLREMR LAMALEKKFT
KDQILEGYLN IVFFNRSAYG IEAAAQYFFS LPASRLTLPQ SALLAGLVNS PSFYDPVANP
KNSLKRRNQV LGEMLKQKMI TKKQHDAAVA SGVGLKVRPS QQGCAAATMA PYFCDYVTRL
FLNNPAYGAD TEAREKRLFR GGLTITTTLD SRLQAKAQAQ VNATAGANPD RWGASLVTVQ
PGTGRVLAMA QNTVYLPQPG KFDTQLNFNV DAKDAIGNDL NGAGGFQPGS TMKPFTFAEW
LHQGKTMTTV VDASKREYPL GFRWRSSCGK VAGGYSTKQR RAGLETADDL QNASEGYYRK
MPADYGLYNS INTATFAEAA QLDFCGIQNM VNAVGLRSGL DGTPIDMHQL GNLLGGTGVA
PLTMANAFAT FAADGRYCVP VALAGVADMA GKKLPAEVQK CSETVDKNVV RGVNKALQDM
LNKGSGIYIN PKVQKSVPVA AKTGTNNSNG ATWVLGYTTG LATASFFGDA LEGQQRPGRN
ITIKGTHYDR IDGYMIAGPQ WANYMLQVAR LYPAAAFPKP PASIVSKPAA KPKAPARPAP
KPTAKPKPKD
//