ID A0A0H1ASA7_9GAMM Unreviewed; 393 AA.
AC A0A0H1ASA7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peptidase S1A alpha-lytic prodomain domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=WQ56_03415 {ECO:0000313|EMBL:KLJ01930.1};
OS Luteimonas sp. FCS-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=1547516 {ECO:0000313|EMBL:KLJ01930.1, ECO:0000313|Proteomes:UP000035397};
RN [1] {ECO:0000313|EMBL:KLJ01930.1, ECO:0000313|Proteomes:UP000035397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCS-9 {ECO:0000313|EMBL:KLJ01930.1,
RC ECO:0000313|Proteomes:UP000035397};
RA Bala M., Kumar A., Kaur N., Mathan Kumar R., Kaur G., Singh N.K.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Luteimonas oceanisediminis
RT sp. nov., a novel gammaproteobacteria isolated from a marine sediment.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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:KLJ01930.1}.
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DR EMBL; LASZ01000003; KLJ01930.1; -; Genomic_DNA.
DR RefSeq; WP_047135691.1; NZ_LASZ01000003.1.
DR AlphaFoldDB; A0A0H1ASA7; -.
DR STRING; 1547516.WQ56_03415; -.
DR PATRIC; fig|1547516.3.peg.728; -.
DR Proteomes; UP000035397; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd21112; alphaLP-like; 1.
DR Gene3D; 3.30.300.50; -; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR037295; Alpha-lytic_protease_prodomain.
DR InterPro; IPR004236; Pept_S1_alpha_lytic.
DR InterPro; IPR001316; Pept_S1A_streptogrisin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR035070; Streptogrisin_prodomain.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF02983; Pro_Al_protease; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001134; Streptogrisin; 1.
DR PRINTS; PR00861; ALYTICPTASE.
DR SUPFAM; SSF54806; Alpha-lytic protease prodomain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001134-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000035397};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..393
FT /note="Peptidase S1A alpha-lytic prodomain domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002591436"
FT DOMAIN 119..182
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 222..368
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 338
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT DISULFID 210..230
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 296..306
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 332..365
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 393 AA; 41133 MW; 1B97F9FBB87ED660 CRC64;
MHTLHAAVRR TLALALLSAA AAGGSALAAQ PGLPSLDPGM VAALERDLGM TQDQYRVTVD
AERRVPTVET AARQLYGDSY AGTWIEHDAD GQPRLVVATA ARDKRLPAVD GADVRQVRYS
LYELDQAVHA LDQSATSRIM RRLDGVQSWG VDLPNNRVVV TLSPGAGRAE AVLDFLARSD
VDTGALHFEV SEQVPSTLIN IYGGIQYNTC SIGFPVTRGS TKGFVTAGHC GSAGTAVRIG
GTTVGSFQAS NFPGSDAAWA TVRQQDTLFG RVWQYSGSTT TPVVGSAEAA VGAAICRSGY
RTGWRCGTIT RTNVSVTYAQ GTVNGLRESN ACAGQGDSGG SWISSAGHAQ GVTSGGALGT
DGTNCGIAQS QRRSWYQRLT PMLSSYGVTL VTN
//
