ID A0A0N1EW49_9GAMM Unreviewed; 715 AA.
AC A0A0N1EW49;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KPH62223.1};
GN ORFNames=ADS77_13080 {ECO:0000313|EMBL:KPH62223.1};
OS Pseudoalteromonas porphyrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=187330 {ECO:0000313|EMBL:KPH62223.1, ECO:0000313|Proteomes:UP000037848};
RN [1] {ECO:0000313|EMBL:KPH62223.1, ECO:0000313|Proteomes:UP000037848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-SED14 {ECO:0000313|EMBL:KPH62223.1,
RC ECO:0000313|Proteomes:UP000037848};
RA Coil D.A., Jospin G., Lee R.D., Eisen J.A.;
RT "Draft Genome Sequence of Pseudoalteromonas porphyrae UCD-SED14.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-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:KPH62223.1}.
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DR EMBL; LHPH01000014; KPH62223.1; -; Genomic_DNA.
DR RefSeq; WP_054454819.1; NZ_LHPH01000014.1.
DR AlphaFoldDB; A0A0N1EW49; -.
DR STRING; 187330.AMS58_09620; -.
DR PATRIC; fig|187330.3.peg.1044; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000037848; 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; cd07496; Peptidases_S8_13; 1.
DR Gene3D; 2.60.120.380; -; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034176; Peptidases_S8_13.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..715
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005870655"
FT DOMAIN 180..482
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 523..591
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT DOMAIN 633..698
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 216..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 437
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 715 AA; 73308 MW; B27777E40F4BEE11 CRC64;
MTTSTTFKKC AVALTLGTLF AASSSMANPS QVIMPSMADT TAKLQGQSAL GTRFIIKYKN
NSNDMATFSV ADASPQMMNQ KAQGFVSAFT SKKAKVKAQY VRPMALSNHH VMRVDKNLNA
DETQEFMQEM IASGNVEYIE IDQMLQPFAT PNDPRYNDQW HYYEQAGGLN LPTAWDTATG
SGVVVAVLDT GYRPHVDLNA NLLPGYDMIS DTFVANDGGA RDSDARDPGD ATNTGECGTN
QLGQPVPASN QNSSWHGTHV AGTVAAVTNN GEGVAGVAYD SKVVPVRVLG KCGGLTSDIA
DGIIWASGGS VSGVPSNANP ADVINMSLGG AGSCSSTTQS AINQARGNGT VIVIAAGNDN
DNSANYNPGN CSGVVNVASV GRNGGRAYYS NYGSNIDVAA PGGAQSFAND SEGVLSTHNS
GSSSPTGDSY HYSQGTSMAA PHVAGVAALI KQAKPNATPD EIESILKSTT RSFAATCNNC
GTGIVDAAAA VTAASGGTTP PGGNELADGQ AKTGLSGAAN SETFYTMTVP SGATNVTFTM
SGGSGDADMY VRAGSKPTSS TYDCRPYKGG NSEECSIDNP TAGTYHVMLR GYSAYSAVSL
VGNLTTSGGG TGAPQAGGGT VADISASAGQ WKHYTLDVPA GMASFTVTMS GGTGDADLFV
KAGSRPTTSS YDCRPYKNGN AETCTFTNPQ AGTWHLSANA YSTFSGVTID AQYKP
//
