ID J1FFU9_9BACT Unreviewed; 506 AA.
AC J1FFU9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Aqualysin 1 {ECO:0000313|EMBL:EJF09134.1};
GN ORFNames=O71_16891 {ECO:0000313|EMBL:EJF09134.1};
OS Pontibacter sp. BAB1700.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1144253 {ECO:0000313|EMBL:EJF09134.1};
RN [1] {ECO:0000313|EMBL:EJF09134.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB1700 {ECO:0000313|EMBL:EJF09134.1};
RX PubMed=23105068; DOI=10.1128/JB.01550-12;
RA Joshi M.N., Sharma A.C., Pandya R.V., Patel R.P., Saiyed Z.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Pontibacter sp. nov. BAB1700, a Halotolerant,
RT Industrially Important Bacterium.";
RL J. Bacteriol. 194:6329-6330(2012).
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:EJF09134.1}.
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DR EMBL; AKIS01000123; EJF09134.1; -; Genomic_DNA.
DR RefSeq; WP_007658242.1; NZ_AKIS01000123.1.
DR AlphaFoldDB; J1FFU9; -.
DR PATRIC; fig|1144253.3.peg.3337; -.
DR Proteomes; UP000003746; 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 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; 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; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
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};
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..506
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003742904"
FT DOMAIN 53..138
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 269..481
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 141..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 311
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 469
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 506 AA; 52759 MW; 78A7FCEF481BBCD6 CRC64;
MMNNSTLFKA LSGLALASVF TLSSCQKEDF MEEQFQTDSV QVDTQHGQAI PGQYIVVFKN
GGNNLSATGV SGMTVAGRTA TVALRERMLL TAGIEREAIQ QTFEGNVNGF AARLSKDQLD
QLRKNPEVAY VEQDRIIMLA KPGTDNTTTK GNGKTKDDST TTKGNGKTKD DSTTTKGNGN
GNGNGKNKNT EPAPTEPAPS EPTPTEPIPT EPAPTEPEPT EPTPTEPTPT EPSPEPEPEQ
PTSSPYAKIT PLPGETLPWH IAMNGYGDGT GKTVWVIDSG IDTDHPDLNI DFQRSTSLIY
GDASIEDGFG HGTYVSGIIA AKNNGTGMVG VAANANVVAL RVFDNTGYGT VSRAISAVNY
VTNMAKPGDV VNMSLGSGIS STLDNAVTTA AGRGILFAIA AGNSAVDCSV NSPARVNAPG
VYTVSAMDRY QNFWSSSNYG APVDYTAPGV SVTSTRIGGG IGSVGSGTSF AAPHVAGILL
LRGEVFSQGI VNGDKDSWPD PIASVE
//
