ID A0A0Q5LI00_9MICO Unreviewed; 610 AA.
AC A0A0Q5LI00;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF00326};
GN ORFNames=ASF82_13180 {ECO:0000313|EMBL:KQR44399.1};
OS Frigoribacterium sp. Leaf164.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR44399.1, ECO:0000313|Proteomes:UP000051005};
RN [1] {ECO:0000313|EMBL:KQR44399.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR44399.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR44399.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR44399.1,
RC ECO:0000313|Proteomes:UP000051005};
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00008645}.
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:KQR44399.1}.
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DR EMBL; LMOX01000003; KQR44399.1; -; Genomic_DNA.
DR RefSeq; WP_056059197.1; NZ_LMOX01000003.1.
DR AlphaFoldDB; A0A0Q5LI00; -.
DR STRING; 1736282.ASF82_13180; -.
DR OrthoDB; 9805123at2; -.
DR Proteomes; UP000051005; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR22946; UNCHARACTERIZED; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051005};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..610
FT /note="Peptidase S9 prolyl oligopeptidase catalytic domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038923500"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 485..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 520..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 553..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..194
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 610 AA; 66294 MW; 0FA19A2771C5DE21 CRC64;
MKPTLIRRNG FWLALSLVLM ALSSIVSSAV QTSGYAVSVK DMNWETASGQ SMSALLYKPN
GVSADDQAPA IVVSHGWWNN KEMQDANYVE LARRGYVVVS IDMYGHGDSD YLPATNLELG
GTGMYDAVKL VADLPYVDPD KIGVSGHSNG ARAANFSVAL DNEADEQLID AVFLVDNDPV
YVDADGAYTN IYGDRDTGLV ADQYDEFFFR SYDADGVALT APRDYIGTPN AQSFLNHGVE
PAEDGDVREA NTLYDDDSLR VVYTPAQTHP WGTISKQTVS DQLEFWEASF GAPEPIDSGS
QIWQVKEAFT ALGLIGFMIF LLAFARALLT TRAFAELRTD AVPVAANTRR GLGWFWGGMI
VSAVVSGVSY VALSQSPWIN SIAFNAAPTP FTQGATFFIA FWAAVNGVAA IAIMVISYLL
FGRKNGVEVR DLGLLPGGRK LLKSVGLAAV TVAAAFGLVF LSDWLLHTDY RFWVVAVKDF
EPDKLWVALL YLPFFLVYFV ANSVAINVFN RFTFRGREWV NTAVLALVNA SAPIVLVVAQ
YTTFFITGET IPGFGGIFSI WLFPVIVILA ATAVLSRKLY RVTGNPYVGG FISAAVVTLV
SVTNTLTVTY
//
