ID L8J9Y9_9GAMM Unreviewed; 522 AA.
AC L8J9Y9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Serine metalloprotease {ECO:0000313|EMBL:ELR64354.1};
GN ORFNames=C942_02627 {ECO:0000313|EMBL:ELR64354.1};
OS Photobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1056511 {ECO:0000313|EMBL:ELR64354.1, ECO:0000313|Proteomes:UP000011134};
RN [1] {ECO:0000313|EMBL:ELR64354.1, ECO:0000313|Proteomes:UP000011134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK15 {ECO:0000313|EMBL:ELR64354.1,
RC ECO:0000313|Proteomes:UP000011134};
RA Khatri I., Vaidya B., Srinivas T.N.R., Subramanian S., Pinnaka A.;
RT "Genome Assembly of Photobacterium sp. AK15.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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:ELR64354.1}.
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DR EMBL; AMZO01000029; ELR64354.1; -; Genomic_DNA.
DR RefSeq; WP_007468411.1; NZ_AMZO01000029.1.
DR AlphaFoldDB; L8J9Y9; -.
DR MEROPS; S08.067; -.
DR PATRIC; fig|1056511.3.peg.3703; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000011134; 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:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; 1.
DR CDD; cd07496; Peptidases_S8_13; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 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; 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; IPR034176; Peptidases_S8_13.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Metalloprotease {ECO:0000313|EMBL:ELR64354.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..522
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003992885"
FT DOMAIN 472..518
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 390
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 522 AA; 55885 MW; A606EF8C218D6D1F CRC64;
MRTIPTATAL AVLIASCPAL AQNNELITDQ IIVKYRSHSP VMLTESATDN SVAHLQQITD
SEVLYVRPSS NNTHVLRVPD QQNLDTVIEQ LRQDPNIEYA EPDRIMWPTA IPDDPGYSLQ
WHYSSAVSGI NMPKAWDITT GSPDVVVAVI DTGVRFDHPD LMNNLLPGYD FIKNAAGARD
GDGRDADATD EGDWLVAGQC GRNYPPRDRN SSWHGTHVAG TIAAEGNNGQ GVTGVSWNTR
ILPVRVLGAC GGYTSDITDG MRWAAGLSVP GAPANSYPAQ VLNLSLGGQG ACGYTYQQTV
NEVRAAGATV VVAAGNDNLN VRDFNPGNCQ GVISVAANNK EGNRAFYSNF GDMIDITAPG
GGRSEGILST YNTGKRQAEK NSYNYSMGTS MATPHVAGVA ALMYSLDASL TPDQVEQYIK
ETARPFPAGS TCNTAICGTG IIDTLAVLER VKGIQPTPKP NPQPGTVDCS NMTLWSPNNV
YQAGDQIQLN GVAYEAKWWS QNQSPADNSS DWGVWTELGQ CK
//
