ID A0A1M7J7S3_9FLAO Unreviewed; 585 AA.
AC A0A1M7J7S3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Protease-4 {ECO:0000313|EMBL:SHM49066.1};
GN ORFNames=SAMN05444484_106212 {ECO:0000313|EMBL:SHM49066.1};
OS Flavobacterium chilense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=946677 {ECO:0000313|EMBL:SHM49066.1, ECO:0000313|Proteomes:UP000184028};
RN [1] {ECO:0000313|EMBL:SHM49066.1, ECO:0000313|Proteomes:UP000184028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24724 {ECO:0000313|EMBL:SHM49066.1,
RC ECO:0000313|Proteomes:UP000184028};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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DR EMBL; FRBT01000006; SHM49066.1; -; Genomic_DNA.
DR RefSeq; WP_068844156.1; NZ_LSYT01000008.1.
DR AlphaFoldDB; A0A1M7J7S3; -.
DR STRING; 946677.SAMN05444484_106212; -.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000184028; 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:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd07018; S49_SppA_67K_type; 1.
DR CDD; cd07023; S49_Sppa_N_C; 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, ECO:0000313|EMBL:SHM49066.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 120..271
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 368..518
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 188
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; 64739 MW; BF053E31B1808063 CRC64;
MKFLGNVIAT VIGIFVFIML FFFGVILIGA IFGGDDSVSV KSDSVIELNL KQIKNDYAGK
YKDPWITVFS DKKEIGLTDV INAIEAAKKD DKIKGISILN DESSLGLAQY KDLRNALESF
KKSGKFVWAY ANTYSQKEYY LNSVANTIYL NPAGDLDFKG LSSEVMFFKD FQDKTGIHME
VIRHGKYKSA VEPFLENKMS DANREQVTAL LNSIWTTVST DISKSRNIPL PKLNEIANGL
LARTPEMAKA QHLVDIVAYE DVYHDAIKKA LKVTGDDDYN KISILDYTQN NITTALTNTA
TDQIAIIYAQ GEIQSGEGDV TVIGEGSMRR SLQEARKNDD VKAIVLRIDS PGGSALTSDL
IWREIEITKK VKPVVVSMGN YAASGGYYIA CNANTIFAEN NTITGSIGVF GILPNFSPLA
NKLGINTEQV KTHENSANYS PFVPVDEKFK AFTLEGVEHI YNTFVTHVAE GRKMTFAQVD
AIAQGRVWSG TEAVKIGLVD KIGGLNDAIA EAARIAKIKT YSTQNYPEYE KTLNDLLSNL
PFAQSKEAFI KEEIGEENYM LIEQVKRLQK QKGVQAMLPF GLNIK
//
