ID A0A0S9DZ91_9MICO Unreviewed; 814 AA.
AC A0A0S9DZ91;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=PASTA domain-containing protein {ECO:0000259|PROSITE:PS51178};
GN ORFNames=ASF06_00595 {ECO:0000313|EMBL:KQO11212.1};
OS Agreia sp. Leaf244.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agreia.
OX NCBI_TaxID=1736305 {ECO:0000313|EMBL:KQO11212.1, ECO:0000313|Proteomes:UP000051484};
RN [1] {ECO:0000313|EMBL:KQO11212.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf244 {ECO:0000313|EMBL:KQO11212.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO11212.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf244 {ECO:0000313|EMBL:KQO11212.1};
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:KQO11212.1}.
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DR EMBL; LMLX01000001; KQO11212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S9DZ91; -.
DR STRING; 1736305.ASF06_00595; -.
DR Proteomes; UP000051484; 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; 1.
DR Gene3D; 3.30.10.20; -; 1.
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; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
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}.
FT DOMAIN 675..741
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 707..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 85000 MW; 1D3490B5AE1A143A CRC64;
MVAPALAVTG IATNNSIGMF ENLPSNIRPD VLAQKSEIYA TGSDGTPVLL ASVFDQNREE
VSWDQISPFV KDAVVSVEDP RFYTHGGVDI ISAARAAAQS AAGGDGPGAS TISMQYVRNI
LIQKTEEIQD EAERDKAFED ATKTTVDRKL KEMKLAIGLE KEFTKDQILL GYLNISNFGG
TVYGIEAAAQ YYYGVSAKDV SLAQAASLVA MVNEPNGLRI DQPDAPEKIT ENQARRDVNI
LPAMLKEHKI TQAQFDEAIA TPVTPNIVQP STGCKTANPN YGAGYFCDYV SYIVKNDPAF
GDSAEARWQK FRTGGYQIFT TLDLDLQTAA INSMNSNVPQ VADQLNLGSA MVTVQPGTGK
VLAMVQNKTF NDDPETTQPN ETSLNLSTDY AYGGSTGFPS GSTYKVFTLA DWLKTGHSLN
EQVNGSVRTF NLATFKNRCE GSGGGPYKSA NDGSANPGSM SVTAATAASV NNAYIGMAQK
LDMCDITETA ESFGMHRADG TPMQQNVSSV LGTNEVAPLT VAAAYAGIAA NGLYCQPKAI
DRILDATGAD VPIPETTCTQ AVDPNVAAAM DVAMAAVVNG GTGGAARPGD GIPLIGKTGT
TDGEKHVWFA GASTTLATAI WVGNIVGDVS VRYTSVPDYG NVADMRFSTW REYMGQANAK
FPGGAFPTPN SSLTATPQIA VPAVQGKTIA EAQSLVEAAG FTFQDGGATD NEAPAGTAAG
SVPAGGTEAT KGSTVTVYTS NGALKSVPDV VSGSNTLGEA ANKLGPAGWK FAGTKYQVTG
DGCDEKKPIG TEPAVGSYAN PATTGVYVIG CKKK
//
