ID F7ZIE6_ROSLO Unreviewed; 386 AA.
AC F7ZIE6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Putative subtilase family protein {ECO:0000313|EMBL:AEI92465.1};
GN OrderedLocusNames=RLO149_c004370 {ECO:0000313|EMBL:AEI92465.1};
OS Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC
OS 15278 / OCh 149).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=391595 {ECO:0000313|EMBL:AEI92465.1, ECO:0000313|Proteomes:UP000001353};
RN [1] {ECO:0000313|EMBL:AEI92465.1, ECO:0000313|Proteomes:UP000001353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149
RC {ECO:0000313|Proteomes:UP000001353};
RX PubMed=21693016; DOI=10.1186/1471-2164-12-324;
RA Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., Wollher A.,
RA Daniel R., Simon M., Brinkhoff T.;
RT "Comparative genome analysis and genome-guided physiological analysis of
RT Roseobacter litoralis.";
RL BMC Genomics 12:324-324(2011).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002623; AEI92465.1; -; Genomic_DNA.
DR RefSeq; WP_013960406.1; NC_015730.1.
DR AlphaFoldDB; F7ZIE6; -.
DR STRING; 391595.RLO149_c004370; -.
DR KEGG; rli:RLO149_c004370; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_21_0_5; -.
DR Proteomes; UP000001353; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05561; Peptidases_S8_4; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 143..376
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 386 AA; 40187 MW; 18ED9B2D5698134C CRC64;
MINALQFLRQ VVIISLLFVL VGCAPLTTSP DKNDTNVVGQ RKVIALVPDA QATEGMRAAG
LSGGYQLLDV TDLAGLDLTM LTFRMPDGIT GPQAIAALEA AVPTSTVGIN HAYRLQQSSS
AAQELDYANA MMRWRTDGCR AQVPVGVIDT GIDTTSPALD GARIVTRAFF EGRAAPAAHG
TDVASVLANP SRLKDVTIYG ANVFGQQDAL GLKAGADALV RALDWLAEED VRFVNLALAG
PYNKLLDLAV ERSVDRGLIL VAAVGNDGPN VDPLYPAGFD GVIAVTAVDA DGRIYRNAVR
GPHVDIAAPG VDILVPSGGS VRFVTGTSIA TPLITARLAA DPTLANARSV SDVRKRLAAT
SAELGRSGRD PVYGHGLALA EDICGD
//
