ID A0A087MJS4_9GAMM Unreviewed; 665 AA.
AC A0A087MJS4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Acyl-peptide hydrolase {ECO:0000256|ARBA:ARBA00032596};
DE AltName: Full=Acylaminoacyl-peptidase {ECO:0000256|ARBA:ARBA00032284};
GN ORFNames=N788_11415 {ECO:0000313|EMBL:KFL37127.1};
OS Arenimonas donghaensis DSM 18148 = HO3-R19.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1121014 {ECO:0000313|EMBL:KFL37127.1, ECO:0000313|Proteomes:UP000029085};
RN [1] {ECO:0000313|Proteomes:UP000029085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO3-R19 {ECO:0000313|Proteomes:UP000029085};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas donghaensis.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFL37127.1, ECO:0000313|Proteomes:UP000029085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO3-R19 {ECO:0000313|EMBL:KFL37127.1,
RC ECO:0000313|Proteomes:UP000029085};
RX PubMed=26380644; DOI=10.1186/s40793-015-0055-4;
RA Chen F., Wang H., Cao Y., Li X., Wang G.;
RT "High quality draft genomic sequence of Arenimonas donghaensis DSM
RT 18148(T).";
RL Stand. Genomic Sci. 10:59-59(2015).
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228}.
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:KFL37127.1}.
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DR EMBL; AVCJ01000007; KFL37127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087MJS4; -.
DR STRING; 1121014.N788_11415; -.
DR PATRIC; fig|1121014.3.peg.1037; -.
DR OrthoDB; 4269629at2; -.
DR Proteomes; UP000029085; Unassembled WGS sequence.
DR GO; GO:0008242; F:omega peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR42776:SF27; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 6; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000029085};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..665
FT /note="Acyl-peptide hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001826301"
FT DOMAIN 115..370
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 443..649
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 665 AA; 72459 MW; F0001252F25A11C9 CRC64;
MSVASRTALT LSIAVSLSLG LAACQQSPAP SPGTGTEAKT AAETVARPSR QYDIEEFVES
TGVGGASFSA DESRILFSSN KSGVWNAYTM PAQGGEWTAV TNSDTDNIYS EAFFPNDDRV
LVSRDQGGNE LDHLYVIEAD GSERDLTPGE NLKAGFMGFG HDGQSFFVIS NERDPRFFDV
YRYDADDYER ELVYRNEAGY EPGEISPDGR WLALGETHTT NDSDLHVVEL ATGEVTKVSE
HEGQAQFAAE AFSPDGAWLY YTANDRGEFA GLRRVNLATW AHEPVRSADW DIVDAALSHD
GTYLAVATNV DGSTGVQLFE TATGEEVALP DFPAGEVRNL RVSRSEDKLA FYLNGDRQPN
DLYVLDLAAG GEPKQLTTSL NPAIDPADLV DSRVVRFDSF DGMPIPNILW KPHQANADNP
VPALVWVHGG PGGQTTRAHS PLIQYLANHG YVVLGINNRG SSGYGKTFFA ADDGKHGREP
LWDTVEAKKY LQSLDYVDDD RIGIIGGSYG GYMVLSALAF QPGEFKVGVN IFGVSNWLRT
LESIPPYWES FREALYQEIG NPETQRDFLI ETSPLFHADK INVPLMVLQG ANDPRVIKPE
SDDIVAAVEK NGVPVEYVVF DDEGHGFSKK KNQIEGYGRI LAFLDTHLKT ATPADASPAD
AAPAE
//
