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Database: UniProt
Entry: A0A1F1Q9N8_9PSED
LinkDB: A0A1F1Q9N8_9PSED
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ID   A0A1F1Q9N8_9PSED        Unreviewed;       330 AA.
AC   A0A1F1Q9N8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Peptidase S49 {ECO:0000313|EMBL:OFS73399.1};
GN   ORFNames=HMPREF3173_11765 {ECO:0000313|EMBL:OFS73399.1};
OS   Pseudomonas sp. HMSC08G10.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1581141 {ECO:0000313|EMBL:OFS73399.1, ECO:0000313|Proteomes:UP000179079};
RN   [1] {ECO:0000313|EMBL:OFS73399.1, ECO:0000313|Proteomes:UP000179079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMSC08G10 {ECO:0000313|EMBL:OFS73399.1,
RC   ECO:0000313|Proteomes:UP000179079};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S49 family.
CC       {ECO:0000256|ARBA:ARBA00008683}.
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:OFS73399.1}.
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DR   EMBL; LWMZ01000046; OFS73399.1; -; Genomic_DNA.
DR   RefSeq; WP_070573261.1; NZ_KV793306.1.
DR   AlphaFoldDB; A0A1F1Q9N8; -.
DR   OrthoDB; 9764363at2; -.
DR   Proteomes; UP000179079; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd07023; S49_Sppa_N_C; 1.
DR   Gene3D; 6.20.330.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR002142; Peptidase_S49.
DR   InterPro; IPR047272; S49_SppA_C.
DR   PANTHER; PTHR42987; PEPTIDASE S49; 1.
DR   PANTHER; PTHR42987:SF4; PROTEASE SLR0021-RELATED; 1.
DR   Pfam; PF01343; Peptidase_S49; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        44..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          145..288
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
SQ   SEQUENCE   330 AA;  36791 MW;  AA1BD273F63D0D41 CRC64;
     MADEWRAPEP EESEEREERK SWKLLEKTLL AGVQEQRRAR RWGIFFKLLT FVYLFGLLVL
     FTPMMDVDKA ASRSANHTAL VEVRGMIADE EPASADNIIK SLRDAFKDTK TKAVIMRINS
     PGGSPVQSGY VYDEIRRLRA EYPAIKLYAV IADLGASGAY YIASAADEIY ADKASLVGSI
     GVTAAGYGFV GTMEKLGVER RTYTAGEHKA FLDPFSPQKP EETAFWQGVL DTTHRQFIAM
     VKQGRGDRLK DKEHPELFSG LVWSGEQAKE LGLVDGLGSA SYVAREIVGE KELVDFTVQE
     SPFDRFSKRL GASVAERLAM WMGFQGPSLR
//
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