ID   A0A257R3W7_9PROT        Unreviewed;       704 AA.
AC   A0A257R3W7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=S9 family peptidase {ECO:0000313|EMBL:OYV55312.1};
GN   ORFNames=B7Z76_10840 {ECO:0000313|EMBL:OYV55312.1};
OS   Acidiphilium sp. 20-67-58.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=1970291 {ECO:0000313|EMBL:OYV55312.1, ECO:0000313|Proteomes:UP000216756};
RN   [1] {ECO:0000313|EMBL:OYV55312.1, ECO:0000313|Proteomes:UP000216756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20-67-58 {ECO:0000313|EMBL:OYV55312.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OYV55312.1}.
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DR   EMBL; NCAS01000025; OYV55312.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257R3W7; -.
DR   Proteomes; UP000216756; Unassembled WGS sequence.
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; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR   PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          12..421
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          486..701
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   704 AA;  76548 MW;  0C40FB7762806995 CRC64;
     MNTPNPPHPT PPAAARKPVR IEQLGRVRTD DYAWLRDANW QAVLRDPAAL DPEIRAHLLA
     ENAYTDAVLA GTRDLQATLL AEMKGRIKDD DSTVPAPHGA YAYYRRYDPG AEHPVIARTP
     RAGGAEQILL DLPARAKGHA FFSAPAVAHS EDHRLLAWAE DTQGSEVYRI HVRVIETGAE
     PAPPIESCSG DFTFSPCARF IFWVFRDDHG RPTKIFRRAL ADGSDTLVYA EPDPGFFLGV
     ETSLSGGSIL VSAGNQDTSE VWRIPGNDPT APPALIAPRE PGLRYDVEDA GDRLIIRTNA
     DGAVDFKLVE APLDTPLDAP LDSLGRAHWR DLVPHRPGRY LVGAFALKHH IVRLERIEAN
     TRIIVAPRDG GAEWEIAQDE PAYVLRAESG LEYDTGTIRY VYSSPTTPRQ TFDYDLATRT
     PILRKTQDIP SGHDPARYET RRIDAMAADG ASIPVTVLMR RGQALDGAAP LLLYGYGAYG
     IPMEPWFRTS ILSLVDRGWI FAIAHVRGGT EKGWNWFLGG RAAHKMNSFT DFTAAAEALI
     GGGYARAGNI VAQGGSAGGL LVGAAFTMRP DLWAGVIAEV PFVDVLNTIS DDTLPLTPPE
     WPEWGNPITD PAAYDTIAAY SPYDNLAPRA YPPILCTGGL SDPRVTYWEP AKFIARLRAL
     ATGPAPALLR IDMEAGHAGA AGRFDALKQT ALNYAFALWS VGAG
//