ASPA_AERSA
ID ASPA_AERSA Reviewed; 621 AA.
AC P31339;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Microbial serine proteinase;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=aspA;
OS Aeromonas salmonicida.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=645;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-30; 322-339
RP AND 368-386.
RC STRAIN=MT0004 / U2862;
RX PubMed=1468618; DOI=10.1016/0378-1097(92)90289-z;
RA Whitby P.W., Landon M., Coleman G.;
RT "The cloning and nucleotide sequence of the serine protease gene (aspA) of
RT Aeromonas salmonicida ssp. salmonicida.";
RL FEMS Microbiol. Lett. 78:65-71(1992).
CC -!- FUNCTION: Agent of furonculosis.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X67043; CAA47428.1; ALT_SEQ; Genomic_DNA.
DR PIR; S26691; S26691.
DR AlphaFoldDB; P31339; -.
DR SMR; P31339; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Protease; Serine protease; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..621
FT /note="Microbial serine proteinase"
FT /id="PRO_0000026995"
FT DOMAIN 68..440
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 454..619
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REGION 114..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 354
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 621 AA; 66620 MW; 4A2597290F2C8D7E CRC64;
MRKTSLALAI SALLSALPIA SVQANESCTP LTGKEAGLDT GRSSAVRCLP GINPLQDLLN
SGQNAFSPRG GMAGNDLNLW WAHRTEVLGQ GINVAVVDDG LAIAHPDLAD NVRPGSKNVV
TGGSDPTPTD PDRCPRHSVS GIIAAVDNSI GTLGVAPRVQ LQGFNLLDDN IQQLQKDWLY
ALGQRRHRRQ PGLQPELRMS LVDPEGANGL DQVQLDRLFE QRTQHASAAY IKAAGTAFSR
IAAGNYVAQP HRNLPKLPFE NSNIDPSNSN FWNLVVRAIN ADGVRSSYSS VGSNVFLSAP
GGEYGTDAPA MVTTDLPGCD MGYNRVDDPS TNRLHNNPQL DASCDYNGVM NGTSSATPNT
TGAMVLMAPY PDLSVRDLRD LLARNATRLD ANQGPVQINY TAANGERRQV TGLEGWERNA
AGLWYSPSYG FGLVDVNKTQ PCSRQPRTAA TTGAVALAKG KGNGRSPSAP SRYVGSSPTR
SSTQVDQPLT VEAVQVMVSL DHQRLPDLLI ELVSPSGTRS VLLNPNNSLV GQSLDRQQLG
YVRTKGLRDM RMLSHKFYGE PAHGEWRLEV TDVANAAAQV SLLDRRTNTR STLTEGNNSQ
PGQLLDWSRG YSVLGHDAAR S