ID   Q0AS42_MARMM            Unreviewed;       653 AA.
AC   Q0AS42;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   04-NOV-2026, entry version 102.
DE   SubName: Full=Peptidase S9, prolyl oligopeptidase active site domain protein {ECO:0000313|EMBL:ABI64895.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Mmar10_0602 {ECO:0000313|EMBL:ABI64895.1};
OS   Maricaulis maris (strain MCS10) (Caulobacter maris).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Maricaulales; Maricaulaceae; Maricaulis.
OX   NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI64895.1, ECO:0000313|Proteomes:UP000001964};
RN   [1] {ECO:0000313|EMBL:ABI64895.1, ECO:0000313|Proteomes:UP000001964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10 {ECO:0000313|EMBL:ABI64895.1,
RC   ECO:0000313|Proteomes:UP000001964};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA   Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(alpha)-acetyl-L-alanyl-L-alanine + H2O = N(alpha)-acetyl-L-
CC         alanine + L-alanine; Xref=Rhea:RHEA:83507, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:133520, ChEBI:CHEBI:233105;
CC         Evidence={ECO:0000256|ARBA:ARBA00093986};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83508;
CC         Evidence={ECO:0000256|ARBA:ARBA00093986};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(alpha)-acetyl-L-alanyl-L-alanyl-L-alanine + H2O = N(alpha)-
CC         acetyl-L-alanine + L-alanyl-L-alanine; Xref=Rhea:RHEA:83511,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:133520, ChEBI:CHEBI:195181,
CC         ChEBI:CHEBI:233106; Evidence={ECO:0000256|ARBA:ARBA00093825};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83512;
CC         Evidence={ECO:0000256|ARBA:ARBA00093825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(alpha)-acetyl-L-methionyl-L-alanyl-L-serine + H2O = L-
CC         alanyl-L-serine + N-acetyl-L-methionine; Xref=Rhea:RHEA:83503,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:71670, ChEBI:CHEBI:233101,
CC         ChEBI:CHEBI:233104; Evidence={ECO:0000256|ARBA:ARBA00094004};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83504;
CC         Evidence={ECO:0000256|ARBA:ARBA00094004};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(alpha)-formyl-L-methionyl-L-alanine + H2O = N(alpha)-formyl-
CC         L-methionine + L-alanine; Xref=Rhea:RHEA:83491, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57809, ChEBI:CHEBI:57972, ChEBI:CHEBI:233100;
CC         Evidence={ECO:0000256|ARBA:ARBA00093977};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83492;
CC         Evidence={ECO:0000256|ARBA:ARBA00093977};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(alpha)-formyl-L-methionyl-L-alanyl-L-serine + H2O = L-
CC         alanyl-L-serine + N(alpha)-formyl-L-methionine; Xref=Rhea:RHEA:83495,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57809, ChEBI:CHEBI:233101,
CC         ChEBI:CHEBI:233102; Evidence={ECO:0000256|ARBA:ARBA00093911};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83496;
CC         Evidence={ECO:0000256|ARBA:ARBA00093911};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(alpha)-formyl-L-methionyl-L-leucyl-L-phenylalanine + H2O =
CC         L-leucyl-L-phenylalanine + N(alpha)-formyl-L-methionine;
CC         Xref=Rhea:RHEA:83443, ChEBI:CHEBI:15377, ChEBI:CHEBI:57809,
CC         ChEBI:CHEBI:194314, ChEBI:CHEBI:233080;
CC         Evidence={ECO:0000256|ARBA:ARBA00094095};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83444;
CC         Evidence={ECO:0000256|ARBA:ARBA00094095};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(alpha)-formyl-L-methionyl-L-phenylalanine + H2O = N(alpha)-
CC         formyl-L-methionine + L-phenylalanine; Xref=Rhea:RHEA:83487,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57809, ChEBI:CHEBI:58095,
CC         ChEBI:CHEBI:233099; Evidence={ECO:0000256|ARBA:ARBA00093961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83488;
CC         Evidence={ECO:0000256|ARBA:ARBA00093961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(alpha)-formyl-L-methionyl-L-serine + H2O = N(alpha)-formyl-
CC         L-methionine + L-serine; Xref=Rhea:RHEA:83499, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33384, ChEBI:CHEBI:57809, ChEBI:CHEBI:233103;
CC         Evidence={ECO:0000256|ARBA:ARBA00093892};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83500;
CC         Evidence={ECO:0000256|ARBA:ARBA00093892};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC         polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC         Pro nor hydroxyproline.; EC=3.4.14.5; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU10084};
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DR   EMBL; CP000449; ABI64895.1; -; Genomic_DNA.
DR   RefSeq; WP_011642542.1; NC_008347.1.
DR   AlphaFoldDB; Q0AS42; -.
DR   STRING; 394221.Mmar10_0602; -.
DR   KEGG; mmr:Mmar10_0602; -.
DR   eggNOG; COG0823; Bacteria.
DR   eggNOG; COG1506; Bacteria.
DR   HOGENOM; CLU_008615_3_2_5; -.
DR   OMA; AACVDWL; -.
DR   OrthoDB; 1094230at2; -.
DR   Proteomes; UP000001964; Chromosome.
DR   GO; GO:0008239; F:dipeptidyl-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; 3.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9_cat.
DR   InterPro; IPR002470; Peptidase_S9A.
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   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001964};
KW   Signal {ECO:0000256|PROSITE-ProRule:PRU00303, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..653
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303,
FT                   ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5048868110"
FT   DOMAIN          435..645
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   ACT_SITE        504
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10084"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   653 AA;  71009 MW;  143286DA0D4E4E4F CRC64;
     MKRLTMSTSL ALAGLLAACQ PAGTGTETAE TPPAAAEAAA RHDAATFHQT TSFSLASSAG
     FAWSADDSRI LISSDETGVF NAYAVDPSTG DREALTSSET DATFALSWFP TDDRAVVTAD
     SGGNEISHIF VRELDGRLND ITPGEEVRAQ FLGWSPDGND MWLMTNERDQ SAMDIYAYDT
     LSYESGFVFQ NDDALQIGDV SPDGRWVALV RNRTSADSDI LLLDLASGET EPSVITAHEG
     NIAHGVYTFT PDSTQLVYAT DQHGEFNQAW TYDLADGTTA PLIEADWDVQ FVIYSDSGRY
     QVSGINADAR TEVSILDTMS GETLALPDLP AGDISSVRFS RDEGRIAFLI NSATSPSNIH
     VVDLASQAHA QLTNALNPAI SEAEMVDAQV VRFESFDGLE IPGILYRPHG ASADNPVPAL
     VWVHGGPGGQ SRIGYSATIQ HLVNHGYAVY AANNRGSSGY GKTFFHMDDR RHGEEDLRDI
     VAAGDWLRTQ DWVNAEEVGV IGGSYGGYMT AAALTFHPEA FEVGVNIFGV TNWERTLASI
     PPWWESFREA LYDEMGDPAT DAERHHAISP LFHAENVIRP MLVIQGANDP RVLQVESDEL
     VEAVRANGVP VEYVLFPDEG HGFRRRENRI TASEAYVSFL DTYLREQDET PAE
//