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Database: UniProt
Entry: A0A1C3EPH3_9GAMM
LinkDB: A0A1C3EPH3_9GAMM
Original site: A0A1C3EPH3_9GAMM 
ID   A0A1C3EPH3_9GAMM        Unreviewed;       688 AA.
AC   A0A1C3EPH3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Alkaline serine protease {ECO:0000313|EMBL:ODA35102.1};
GN   ORFNames=A8L45_05340 {ECO:0000313|EMBL:ODA35102.1};
OS   Veronia pacifica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Veronia.
OX   NCBI_TaxID=1080227 {ECO:0000313|EMBL:ODA35102.1, ECO:0000313|Proteomes:UP000094936};
RN   [1] {ECO:0000313|EMBL:ODA35102.1, ECO:0000313|Proteomes:UP000094936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 1920 {ECO:0000313|EMBL:ODA35102.1,
RC   ECO:0000313|Proteomes:UP000094936};
RA   Gomez-Gil B., Enciso-Ibarra J.;
RT   "Genomic Taxonomy of the Vibrionaceae.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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:ODA35102.1}.
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DR   EMBL; LYBM01000006; ODA35102.1; -; Genomic_DNA.
DR   RefSeq; WP_068899997.1; NZ_LYBM01000006.1.
DR   AlphaFoldDB; A0A1C3EPH3; -.
DR   STRING; 1080227.A8L45_05340; -.
DR   Proteomes; UP000094936; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd12215; ChiC_BD; 2.
DR   CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR   CDD; cd00146; PKD; 2.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR013783; Ig-like_fold.
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; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF02839; CBM_5_12; 2.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF18911; PKD_4; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00495; ChtBD3; 2.
DR   SMART; SM00089; PKD; 2.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR   SUPFAM; SSF49299; PKD domain; 2.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS50093; PKD; 2.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000094936};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..688
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008673286"
FT   DOMAIN          410..489
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          548..629
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        186
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        343
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   688 AA;  72084 MW;  DE61CD47B79A173C CRC64;
     MKTSMIKPAA YAGAFALSLL ASSIQAETQQ SPGTEPQRFI VQLNDTHFSA LTAQNVSPEA
     LELAKIELLN QTALTVDAEV IRSLPSVNAM ALMLDADQKA ALDANPNVAF VEVDPKRYLM
     AESEPYGIGM VQADQVSDSM SGNRKVCIMD TGYERGHEDL PNTGITGDDG YGSNDTGNWF
     QDGNGHGTHV AGTIAGLGGN NRGVVGVNPS GLLGLHIVKV FDDSGSWAYG SDLVAAVNQC
     VNAGSNVISM SLGGGGSSNA ERQAFANAKS RGVLSIAAAG NDGNSTKSYP ASYNDVVSVA
     AVDSSGNKAS FSQYNDQVEI AAPGVGVNST YINGGYRALS GTSMATPHVS GVAALIWSYY
     PSCSADKVRQ AMNETAQDRG AAGRDNQFGY GIVKAKDALT KLGLLCEGDI DQKPVAKFTA
     TVNGKSVSFV NESTDDKGIT AFMWKFGDGN TSTQETPRHT YASDGKYTIE LTVTDTKGQK
     GSTSNVVNIG GPVDPTCAAP WSAATSYKVD DEVSYKGYKY KATWWSTGAQ PDVYTNVWKK
     LSVCNGSGGS APIADFGVTA SDLTVTLTDK STDDKGVVSY DWSFGDGGVS VQKNPVYTYQ
     KSGTYTIRLS VKDAEGKTGV KTKSVTVTVG GNTGGCNGVS AWQSGAIYLT GDTVSYNGSK
     FSARWWTQGE EPGTTGQWGV WKSEGSCQ
//
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