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Database: UniProt
Entry: A0A0S8FI21_9GAMM
LinkDB: A0A0S8FI21_9GAMM
Original site: A0A0S8FI21_9GAMM 
ID   A0A0S8FI21_9GAMM        Unreviewed;      1096 AA.
AC   A0A0S8FI21;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   ORFNames=AMJ59_07445 {ECO:0000313|EMBL:KPK60262.1};
OS   Gammaproteobacteria bacterium SG8_31.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK60262.1, ECO:0000313|Proteomes:UP000051321};
RN   [1] {ECO:0000313|EMBL:KPK60262.1, ECO:0000313|Proteomes:UP000051321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_31 {ECO:0000313|EMBL:KPK60262.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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:KPK60262.1}.
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DR   EMBL; LJTI01000010; KPK60262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8FI21; -.
DR   PATRIC; fig|1703405.3.peg.1239; -.
DR   Proteomes; UP000051321; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF17957; Big_7; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1096
FT                   /note="Peptidase S8/S53 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006646168"
FT   DOMAIN          226..619
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          942..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1059..1096
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        942..968
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        235
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        285
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        555
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1096 AA;  113698 MW;  4756EE3A3C949A95 CRC64;
     MGRLGAILFG LFISVPTAPA LSAPAQTAPP SVGHAIHLST ATFRPALGER PATPPGLTIA
     GYGENQRGLY IVQFAGPVRA DWKARIEAAG AEILEYVPDF AFKVRMNPAQ AKQVATHDAV
     SWVGIFQPAF KLRPKTLQEG ERLYRIRTNR DADAAAVRAE VLAAGARLFG GSGQSFVVMA
     DGVQLQAAAR VLEVAWIEPF AFREKHNEYA SGIVGADTAR ANGFDGAGQI VAIADTGLGN
     GTAGGAHPGI DPGRVAAIHD LVGVSDDPSC YQVVDDGAHD VDSGHGTHVA VSAVGAGNAA
     GVGEGTAPGA ELIFQAVENL TEFVGGCGLF FANGYYLFGI PYDIRELFQQ AYDGNARIHS
     DSWGSPNLGQ YDIDSFYVDD FMWHHPDMTI TYSAGNSGDD FDYDGYTDIA VTSGPDERYY
     LSTPATAKNL ITVGASENDR QGDYACDPVA TNCTGMNELF WYGYAWPLEF GIGPIAGDLT
     AGNAEQMAGF SSRGPTHDNR IKPDLVAPGT WILSGYSDMY QEFYDPAPNP ETGLWQLGGW
     FDPLNAEYKY FGGTSMATPL VAGGAAVVRQ YYQVLYGHDA SAALVKATLV NSAVDLLDEN
     NDGQDDNDIP IPNNHEGWGR MNLDRATDGS HVFEEAVTGL RTGDNATYQY TVETGGAPFK
     VSLAWTDYPS SEAVARNLVN DLDLQVTGPG GESYIGNNFS GGWSQAGGSP DRTNNLENVY
     VEAAAAGVWS VTVSGYNVPN GPQPFALVVD GEMGGIDLPP AVTLTNPTQA ETVAGSILVT
     ANASDHGGVT QVAFAVDSTN IGTDTDGADG WSMPWDTATV DDGSHTITAT ATDTRAQTRS
     DSVEVTVANV VPPPPTVVHV TDMDGASADA GKGSWTATVT IEISEASGAP AVGALIEGTW
     GGSANGGGSC TTGSGGKCEV ANSVRNKSAA VSFTVGNVSH GSSIYDPGQN TDPETDSDGT
     TITVQKDGGS TEPPAPPAGG PTMHVGDLDR ASSVEPRNRW SASVTVWVHA AADAGEGPLS
     GITVNGSWSS GGGGSCTTGA DGTCTIDRTN LKGNVASTTF SVGDLSDTGG SYSYAPGDNH
     DPDGDSSGTA ITVSQP
//
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