ID S9QR63_9RHOB Unreviewed; 473 AA.
AC S9QR63;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peptidase S49 domain-containing protein {ECO:0000259|Pfam:PF01343};
GN ORFNames=Salmuc_02461 {ECO:0000313|EMBL:EPX82093.1};
OS Salipiger mucosus DSM 16094.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX82093.1, ECO:0000313|Proteomes:UP000015347};
RN [1] {ECO:0000313|Proteomes:UP000015347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX PubMed=25197501; DOI=10.4056/sigs.4909790;
RA Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT clade.";
RL Stand. Genomic Sci. 9:1331-1343(2014).
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:EPX82093.1}.
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DR EMBL; APVH01000027; EPX82093.1; -; Genomic_DNA.
DR RefSeq; WP_020038639.1; NZ_KE557276.1.
DR AlphaFoldDB; S9QR63; -.
DR STRING; 1123237.Salmuc_02461; -.
DR eggNOG; COG0616; Bacteria.
DR HOGENOM; CLU_046540_4_0_5; -.
DR OrthoDB; 266140at2; -.
DR Proteomes; UP000015347; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07022; S49_Sppa_36K_type; 1.
DR Gene3D; 6.20.330.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR033855; Protein_C.
DR PANTHER; PTHR33209; PROTEASE 4; 1.
DR PANTHER; PTHR33209:SF1; SERINE PROTEASE SPPA, CHLOROPLASTIC; 1.
DR Pfam; PF01343; Peptidase_S49; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000015347};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 148..293
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT REGION 301..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 48836 MW; 4E83BE772AB93601 CRC64;
MDYPQLAQRV FHTPLLAAPA KAAAFAAGLG PRLLGAPVQV EGAEPTAATR ARPQASVLDD
RLEDEIRMGR RTPFRSIEGA AVIPITGSLV HRGSFLGESL SGHQSYEGIS AQLTAARESP
MVRGVALEID SFGGEVAMCF ELAEEIRALR AEKPVWAFVS AHAFSAAYAL ASQADRIIIP
RSGGVGSIGV ICMHADYSQR LEDGGIRVTV IAAGARKAEG NPYEPLPEAV RARLAQECED
LRVLFAETVG EGRGAALTAE AALATEAGTF IGQKAVDVGL ADEVASPRAA FERFLAQING
RSVPAPTQAS KQGDQTMSNR TDPQGQQPPQ QAASAPTHQP AASEAPTPAA PTTQAGGDAP
AQPSASAPAQ PGANAPTPDP APAKGASDER TRIAGILNHP EAEGRADLAK SFAFESEMSV
DEAAKHLAAA PKSGSGQTLS AAMDAEATEL DAPPAAGGDA PRMADRMKGR FAN
//
