ID A0A0Q5ASV9_9MICO Unreviewed; 801 AA.
AC A0A0Q5ASV9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=PASTA domain-containing protein {ECO:0000259|PROSITE:PS51178};
GN ORFNames=ASF46_11975 {ECO:0000313|EMBL:KQQ08068.1};
OS Rathayibacter sp. Leaf296.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1736327 {ECO:0000313|EMBL:KQQ08068.1, ECO:0000313|Proteomes:UP000050868};
RN [1] {ECO:0000313|EMBL:KQQ08068.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ08068.1,
RC ECO:0000313|Proteomes:UP000050868};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ08068.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ08068.1,
RC ECO:0000313|Proteomes:UP000050868};
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:KQQ08068.1}.
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DR EMBL; LMNR01000002; KQQ08068.1; -; Genomic_DNA.
DR RefSeq; WP_056867806.1; NZ_LMNR01000002.1.
DR AlphaFoldDB; A0A0Q5ASV9; -.
DR STRING; 1736327.ASF46_11975; -.
DR Proteomes; UP000050868; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000050868};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 712..779
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 744..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..801
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 83760 MW; D17A689055DC913D CRC64;
MSGAGGTRVV KSIGGAVGGL IGVVAMSVIA GILVAASITP AIALGGMAAN NGVQMFDNLP
EYLEIGTLAE KSNIYAKDAS GADVLLASFY AQNRVEVGWD DISPFVKDAV VASEDPRFYE
HGGIDLLGTV RAAATTAMGG RVQGGSSITQ QYVKNVLVQK AEALSDPIER DAAYREATET
TPERKVAEMR LAIGLEKEYP KNDILLGYLN IALFGGTVYG IEAAANYYFG TSARDLTLAQ
SAALIAIVNN PEKFRFDRPD DPANLAVEGY PETLNRRNYI LVQMDKESKV TPEQIAEAAG
TPIAPVVTEP STGCQTAGIA AFFCDYVTWV IKNDDAFGAS RDERDATFKR GGYQIYTTLD
SELQQAAVSA TDAWVPKSMG SINIGSSSVS VEVGTGRILA MTQNKDYSND PDVAGPNYTS
VNYSTDFGYG GSSGFQVGST YKVFTLAEWL QEGRSLGESV DGVRRAYTTF RDSCEPDGIY
YGESWDPKND EGGNGGVYSV LDATKGSINT GFAAMAEQLD LCGIRNTALA MGVHRADGTE
LQKFAPTILG TNEIAPLTMA TAFAGFANKG TVCTPIAIDR IVDRTGADVA PPASECTQGM
SEAVAATADY ALQQVMTGGT GRASATGTGV PHIGKTGTTD NAVHTWMVGA STEVATATWV
GNVVGKTSMR GLRLNGVNAG QVRHQIWPRI MRVADAKYGG SAFPSPQRSL VEAPQEAVPE
VTGQSPAAAS ERLRQLGFRV SVDPVRVPSD RPAGTVAQTS PPAGSRIARG SAVVLQVSAG
PATPPPSPTP PSPGTAPPAG G
//
