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
//