ID A0A0Q8CA68_9MICO Unreviewed; 860 AA.
AC A0A0Q8CA68;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ASD61_16610 {ECO:0000313|EMBL:KRA09327.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA09327.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA09327.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA09327.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA09327.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA09327.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRA09327.1}.
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; LMGR01000002; KRA09327.1; -; Genomic_DNA.
DR RefSeq; WP_055825244.1; NZ_LMGR01000002.1.
DR AlphaFoldDB; A0A0Q8CA68; -.
DR STRING; 1736567.ASD61_16610; -.
DR Proteomes; UP000051073; 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 CDD; cd06577; PASTA_pknB; 2.
DR Gene3D; 3.30.10.20; -; 2.
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; IPR005543; PASTA_dom.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PENICILLIN-INSENSITIVE TRANSGLYCOSYLASE; 1.
DR Pfam; PF03793; PASTA; 2.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51178; PASTA; 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:UP000051073}.
FT DOMAIN 783..851
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 627..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 91065 MW; 329231B1DCA37E42 CRC64;
MSAQKRSTSG VLGGFLAFVG MSVAAGVLVT AAVTPAIAVS GMAATNGINM FENLPSYLEI
DELAQKTNVY ATKSDGTPQL LASFFDQDRE EVTWENISQY AKDAAVAGED PRFYEHGGID
VQGTARAMLT TYVLKGDTQG GSSITQQYVK NVLVQKAELE AKTEKEKEAA YAEATDPTPD
RKLKEMRLAI GLEKKYSKDD ILKGYLNIAG FGGRVYGIQA ASQYYFGGVS AKDLKLEQAA
ALLAIVNNPE KFRLDRPDSE TNGAATKVKG EVVPYAATKE RRDYILDSML KYKKITQKEH
DAAIKTPVAP AITEPSTGCS TAADAAFFCD YVYWTILNNE AFGKTQDERK KLLSQGGLDV
YTTLDLDLQH AAADAMFRFV PQSDPNIDVG ATAVSVQPGT GRVLAMSQNK SFSNDSDVLA
LGNNYTAVNY NTDLDYGGSS GFQPGSTYKI FTLAEWIKEG HSLNEYVNAY KRSDWGQFND
SCDGPQNYGG GFAPNNDEGG NGGSWSALFN TVNSENTGFV AMAKQLDLCG IRKTAESFGV
HRADGDPLQQ GASSILGTNE VAPVTMAEAF AGVAASGVVC KPIVIDKIVK QDGTELTPPS
AECAQSVDPK VTSAMAYAMQ RVMWEGTGST SNGRTDPQVP MIGKTGTTDN NEATWMSGAS
TKVATTVGVF NVTGHVNLRD TYFNGTQAAV IRHQIWPAIM SAANAKYGGD GFPDADPSSL
KTVYATVPDV RGKSIQEAQD LIEAAGFAFA DGGAQDSELP AGQVSSTNPS GDAPRGSLVT
VYTSNGAMVL MPDVVGRTEG DAKGQLKGTF SVKSIDVAVT DPKQDGIVQS TDPAAGTGVK
PGSQVTISVG KLKSDKPGKG
//