ID A0A0Q4H9K2_9MICO Unreviewed; 870 AA.
AC A0A0Q4H9K2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=PASTA domain-containing protein {ECO:0000259|PROSITE:PS51178};
GN ORFNames=ASE68_05610 {ECO:0000313|EMBL:KQM82804.1};
OS Agromyces sp. Leaf222.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1735688 {ECO:0000313|EMBL:KQM82804.1, ECO:0000313|Proteomes:UP000050813};
RN [1] {ECO:0000313|EMBL:KQM82804.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM82804.1,
RC ECO:0000313|Proteomes:UP000050813};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM82804.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM82804.1,
RC ECO:0000313|Proteomes:UP000050813};
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:KQM82804.1}.
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DR EMBL; LMKQ01000001; KQM82804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4H9K2; -.
DR STRING; 1735688.ASE68_05610; -.
DR Proteomes; UP000050813; 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; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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; 2.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..870
FT /note="PASTA domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039229496"
FT DOMAIN 715..779
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 783..846
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 845..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 91667 MW; 70F2372084EF5E8D CRC64;
MLAFLGMSAL AGVLVTAAVT PALAVTGMAA NNSITMFENL PGFLKIGELA QKSSIYAIQP
DGTPAEITSF YDDNREEVEF DYISQFLKDA AVAGEDPRFY EHGGIDIKGT LSAVANEFIP
GGATRGGSSI TQQYVKNVLI NNGMNEAKTA EEKQAAYDEA TATTPERKLK EMRYAISIDK
KYPKDEILKG YLNIAAFGGQ VYGVQSAAQY YFKTNAKDLT LPQAASLIAI VNWPEKFRLD
YPDSETNGAN TVVDGEKVPY ADNKSRRDYI LKEMLDEKKI TQEDYDAAVA TPVEPVISPP
TTGCQASPYY AYFCDYVTWE IKDKMDKADT PDVNEGAEML SRGGLKIYTT IDMQMQDVAT
QALKENVPSS IPEMDLGGSV VSVEVGTGRI LAMVQNTDYN VDPDVTGDNY SAVNYNSGID
YGGSSGFQPG STFKTFTLAE WLNEGHSLNE SMNATKRSNW GTFNDSCSGP IDVGGWDPGN
DEGGNGGFWT ALFNTINSEN TGFVAMAKQL DLCGIKKTAT ALMSAGRADG GELGTPAGTD
WTFQPSAVLG TEEVAPLSMA TAFAAFAGGG VSCTPIAIDK IEDAEGNAVE APKSTCTQAI
TTDVAAGMDY ALNKVMTQGT GTSSLYKMDT SGTPMIGKTG TTDNNEATWM SGASSRVATV
VGVYNATGHV NLRQTYVNGE QAAVLRHNIW PRVMDFANTK YPGTGFPEPK SEYLSAPQAE
VPSVLGLTPD AAQKALEAAG FGWALDGEVD SAQPKGTIGE QSATGMTSRG SQIMLKVSKG
NLAPVPNVVG QQADAAEAAL KQAGYKVRRA NENTDDDSKV GIVLSQDPAG DGSAAAGATV
TITIGKKSAG GNDGGNDGDG ETPTVPGGGG
//
