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Database: UniProt
Entry: L7LDH1_9ACTN
LinkDB: L7LDH1_9ACTN
Original site: L7LDH1_9ACTN 
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}.
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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
//
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