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Database: UniProt
Entry: A0A0Q8CA68_9MICO
LinkDB: A0A0Q8CA68_9MICO
Original site: A0A0Q8CA68_9MICO 
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}.
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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
//
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