ID L8TMD7_9MICC Unreviewed; 469 AA.
AC L8TMD7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Subtilisin-like serine protease {ECO:0000313|EMBL:ELT42821.1};
DE Flags: Fragment;
GN ORFNames=G205_22096 {ECO:0000313|EMBL:ELT42821.1};
OS Arthrobacter nitrophenolicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT42821.1, ECO:0000313|Proteomes:UP000011189};
RN [1] {ECO:0000313|Proteomes:UP000011189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJCon {ECO:0000313|Proteomes:UP000011189};
RX PubMed=23516196; DOI=10.1128/genomeA.00058-13;
RA Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.;
RT "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT Arthrobacter sp. Strain SJCon.";
RL Genome Announc. 1:e0005813-e0005813(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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:ELT42821.1}.
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DR EMBL; AOFD01000081; ELT42821.1; -; Genomic_DNA.
DR AlphaFoldDB; L8TMD7; -.
DR Proteomes; UP000011189; 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; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF13517; FG-GAP_3; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF89372; Fucose-specific lectin; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 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}; Reference proteome {ECO:0000313|Proteomes:UP000011189};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..469
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003996431"
FT DOMAIN 50..100
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 138..363
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 327
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 469
FT /evidence="ECO:0000313|EMBL:ELT42821.1"
SQ SEQUENCE 469 AA; 46373 MW; 1DBB1EB2E832C690 CRC64;
MLAAVAAVAL AAQPAAAAIP TAAKPEVPPP ADSGRYLVSF STGADVAQEA ASLRSQGVQV
GRTFSAAVRG AAVTATKAQA AALARSPRVA AVEPDEPVQV FDTQQPAPWN LDRVDQTNLP
LSGTFTPPSS GAGVQAYVVD SGVLAQHTEF GGRVAAGWTA VADGRGSSDC NGHGTHVAGI
VAGQTYGVAK AATIVPVRVL DCNGNGYMSD IVAGLDWVVS HHRAGTPAVA NLSLGGPAST
MVDSAVRGVM ADGITAAVAA GNSGVDACNS SPARVAEALT VAASDSSDRQ ATFSNHGGCV
DLYAPGVGIT SAIHSSTTAA ATVSGTSMAA PHATGAAAVI LSRIPEATPA EVTAELSSTA
TPGVISNASA GTPNRLLNIG AVPAPFPAAR DFTGDGKSDL LARDSGGTLW TYPGTGTGLF
GWRVAVGDGW NVMTSISAAG DLTGDGLPDL LARDSGGTLW TYPGTGNGL
//
