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Database: UniProt
Entry: A0A246ANJ2_9FLAO
LinkDB: A0A246ANJ2_9FLAO
Original site: A0A246ANJ2_9FLAO 
ID   A0A246ANJ2_9FLAO        Unreviewed;       585 AA.
AC   A0A246ANJ2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Signal peptide peptidase SppA {ECO:0000313|EMBL:OWK74480.1};
GN   ORFNames=CBW16_03470 {ECO:0000313|EMBL:OWK74480.1};
OS   Flavobacteriaceae bacterium JJC.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=512012 {ECO:0000313|EMBL:OWK74480.1, ECO:0000313|Proteomes:UP000197808};
RN   [1] {ECO:0000313|Proteomes:UP000197808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JJC {ECO:0000313|Proteomes:UP000197808};
RA   Newman J.D.;
RT   "Genome of Chryseobacterium haifense.";
RL   Submitted (MAY-2017) 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:OWK74480.1}.
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DR   EMBL; NHOS01000001; OWK74480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246ANJ2; -.
DR   OrthoDB; 9764363at2; -.
DR   Proteomes; UP000197808; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd07018; S49_SppA_67K_type; 1.
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; IPR004634; Pept_S49_pIV.
DR   InterPro; IPR004635; Pept_S49_SppA.
DR   InterPro; IPR002142; Peptidase_S49.
DR   InterPro; IPR047217; S49_SppA_67K_type_N.
DR   InterPro; IPR047272; S49_SppA_C.
DR   NCBIfam; TIGR00705; SppA_67K; 1.
DR   NCBIfam; TIGR00706; SppA_dom; 1.
DR   PANTHER; PTHR33209; PROTEASE 4; 1.
DR   PANTHER; PTHR33209:SF1; SERINE PROTEASE SPPA, CHLOROPLASTIC; 1.
DR   Pfam; PF01343; Peptidase_S49; 2.
DR   PIRSF; PIRSF001217; Protease_4_SppA; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          123..265
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
FT   DOMAIN          367..518
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
FT   ACT_SITE        191
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT   ACT_SITE        384
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ   SEQUENCE   585 AA;  65487 MW;  C416ECD62722292B CRC64;
     MRSFVKNVLA NIVAIMIIAA VFFMFLLTLV VVSMFSDSHK ATVKNNSVLT LDFKTNIIDS
     PTEESGELFT FNEKEKNILI FDMLEAIKKA KTDDKIKGIS IETDGIKAGM TQLDDIRTAL
     EDFKKSRKFV YAYGNSVSQS AYYLGSVADQ YFLNPSGGIE LKGLSTEILY MKSFADKYGI
     GIQVIRHGKY KSAVEPFLRD DMSPENKEQL SVLLKDLWSA KSLKMAGSRK MDTAQFRTVV
     DSLYGIIPDL SLQHKLADRL IQKTEYDNLI KAKLNVKEKD KLNKISFSKY ISSFSEDNTK
     KEDQVAVLYA SGAIYNGEGN DAVYSENFVK EIKKLTENDK IKAVVFRINS PGGSANASDE
     ILFEMQQLKK KKPVVVSFGD YAASGGYYIA MAADKIYSEP NTLTGSIGVF GIIPYFKEIA
     NKNGLSSHAV NTNANSNMYS PINGITPGGV SIMTRSVEQT YKRFVHFVTQ NRNKSFTQID
     EVGGGRVWSG TRAKQLGLVD ELGTLNDAIA FAAQKAKIKN YNVATYPKKV TKLEQIFKDM
     DEDEISARLI KNKIGKENYK IFEQVTNPKM KSEVMMEMPY QIKFD
//
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