PROA_VIBAL
ID PROA_VIBAL Reviewed; 534 AA.
AC P16588;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Alkaline serine exoprotease A;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=proA;
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2546861; DOI=10.1016/0378-1119(89)90168-6;
RA Deane S.M., Robb F.T., Robb S.M., Woods D.R.;
RT "Nucleotide sequence of the Vibrio alginolyticus calcium-dependent,
RT detergent-resistant alkaline serine exoprotease A.";
RL Gene 76:281-288(1989).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; M25499; AAA27550.1; -; Genomic_DNA.
DR PIR; JS0173; JS0173.
DR AlphaFoldDB; P16588; -.
DR SMR; P16588; -.
DR STRING; 663.BAU10_17405; -.
DR MEROPS; S08.050; -.
DR eggNOG; COG1404; Bacteria.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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 Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 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; Protease; Serine protease; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..141
FT /evidence="ECO:0000255"
FT /id="PRO_0000027134"
FT CHAIN 142..534
FT /note="Alkaline serine exoprotease A"
FT /id="PRO_0000027135"
FT DOMAIN 57..134
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 148..419
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 423..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 363
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 534 AA; 55931 MW; 84E96D9C649D4226 CRC64;
MLKKLLSCCI TSALCFHSSL AFSQPNEIAD SAELQQAPDT LPATLMLAPD DIAIADRYIV
VFQQPQMMAS SSPEFEQFTQ QSVDRMSGLY SIQVESVFDH SISGFVANLS PEQLKDLRSD
PRVDYIEQDR ILSLDPIVSA DANQTNAIWG LDRIDQRNLP LDNNYSANFD GTGVTAYVID
TGVNNAHVEF GGRSVSGYDF VDNDADASDC NGHGTHVAGT IGGSLYGVAK NVNLVGVRVL
SCSGSGSTSG VIAGVDWVAA NASGPSVANM SLGGGQSVAL DSAVQSAVQS GVSFMLAAGN
SNADACNYSP ARVATGVTVG STTSTDARSS FSNWGSCVDV FAPGSQIKSA WYDGGYKTIS
GTSMATPHVA GVAALYLQEN SSVSPSQVEA LIVSRASTGK VTDTRGSVNK LLYSLTDADC
GQDCGGPDPT PDPEGKLTSG VPVSGLSGSS GQVAYYYVDV EAGQRLTVQM YGGSGDADLY
LRFGAKPTLN AWDCRPFKYG NNETCTVSAT QSGRYHVMIQ GYSNYSGVSI QANY
