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
//