ID L7LDH1_9ACTN Unreviewed; 733 AA.
AC L7LDH1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=GOHSU_53_00070 {ECO:0000313|EMBL:GAC58806.1};
OS Gordonia hirsuta DSM 44140 = NBRC 16056.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1121927 {ECO:0000313|EMBL:GAC58806.1, ECO:0000313|Proteomes:UP000053405};
RN [1] {ECO:0000313|EMBL:GAC58806.1, ECO:0000313|Proteomes:UP000053405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16056 {ECO:0000313|EMBL:GAC58806.1,
RC ECO:0000313|Proteomes:UP000053405};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia hirsuta NBRC 16056.";
RL Submitted (DEC-2012) 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:GAC58806.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BANT01000053; GAC58806.1; -; Genomic_DNA.
DR RefSeq; WP_005943537.1; NZ_BANT01000053.1.
DR AlphaFoldDB; L7LDH1; -.
DR STRING; 1121927.GOHSU_53_00070; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000053405; Unassembled WGS sequence.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF34; PENICILLIN-BINDING PROTEIN 1A; 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:UP000053405};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..253
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 350..613
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 649..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 77690 MW; F6EC1BE2390DE3F0 CRC64;
MSSETKKTDR SPQADRTRVS RIVAWVLGLG AAVVPVVAII GVVAFLLTYM AVDVPAPGDL
KQNQVATITD SKGNVLARVV PPEGNRIDVK YSQIPESMIE AVKAAEDRDF DSNSGFSIRG
FSRAALGKLT GNAGAGGGST ITQQYVKNAM VGDQASGLAG YKRKFKELAI STKMSSQWSK
EDIMTAYLNT IYFGRGAYGV AAAAKAYFGK EVSKLTVSES ALLAAVIRGP SIYDPAVDEQ
LARQRWDYVL EGMVKIDAIS QAEKNAQAFP KTITPKPIGE DEESKGPNGL IKRQVLAELD
KLGISEQEVR TGGLKITTAI DPKVQEALED ASKSKMTGEP KDLRTASVSV DPSTGGISGY
FGGWDGAGWD YASTGLQTGS VFKTFALIAA LEQDIPLSKQ YSSDPYRTSS GLLVENSDGE
SCGTCNLATA MKMSLNTVYY RLMMDLKNGA DDVVDAAHKA GISETINGEK SLRNANGRTE
GGVVLGQYDS TVLDMASSYA TLAASGIYRE PFFVKKVETS DGQTLFDRQP NPGKRVFAAK
VADNVTAALE PIAAYSGGNS LYDSSYGARP SAAKTGTAQL GTSGQNRYSW MVGYTPQLST
AVWVGTARGD KPLVNYGGAA IYGSGLPSQI WKAAMDQALA GETIESFPTP AAVGGQAGVP
YEPPPYTPPP SSSWARPSRP TLPSIDVTIP PEWNIPGLPT RQRPNRPGRT PSEQGETVPE
TPSEPETGEV PAA
//