ID F4G5J9_ALIDK Unreviewed; 732 AA.
AC F4G5J9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:AEB84175.1};
GN OrderedLocusNames=Alide2_1789 {ECO:0000313|EMBL:AEB84175.1};
OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Alicycliphilus.
OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB84175.1, ECO:0000313|Proteomes:UP000007938};
RN [1] {ECO:0000313|EMBL:AEB84175.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RX PubMed=21742888; DOI=10.1128/JB.00365-11;
RA Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA Smidt H., Stams A.J.;
RT "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL J. Bacteriol. 193:5028-5029(2011).
RN [2] {ECO:0000313|EMBL:AEB84175.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073}.
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DR EMBL; CP002657; AEB84175.1; -; Genomic_DNA.
DR AlphaFoldDB; F4G5J9; -.
DR STRING; 596154.Alide2_1789; -.
DR KEGG; adk:Alide2_1789; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_020472_0_0_4; -.
DR OrthoDB; 9768989at2; -.
DR Proteomes; UP000007938; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04847; Peptidases_S8_Subtilisin_like_2; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034074; Y4bN_pept_dom.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007938};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 202..539
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
SQ SEQUENCE 732 AA; 80423 MW; D3E49F9792C0A8C8 CRC64;
MAEDVGGFDD RKLLKIRLRA GDKSVPAFDA IPGVEIVSQE DESIVLAFAT DDGLSEFESR
LATLARDGVV TRKELFYVIE DFDHWTPQDR TGAALLEQGF PAAPTFMLDV ELWPQERQDK
RQQMVRAFLD WLHAQGIERL DDIQQPSLVM VRVRCNGAQA EQILHHRDVR TADLPPRLGV
AVQLLHTDIN QFPPIDPPSD DAPSIAVLDS GLTRGHSLLG AAVGDAQGYL APHRSADDTD
PHWHGTFVGG LALYGDVHGV IQQGQFVPQL RLFSGKVFED DGQDQTEFVE KAVEEAVREL
HAQYGCRVFN LSYGDLNKVY DGRHVRGLAY TLDRLTRELG VLFVVPAGNL LSSQLPADTR
ASYPDYLFEG HARLLDPATS LNALTVGGLS LNEATRNAQR HPNTIEDHVL ARAEQPFPLT
RSGPSASGAI KPDVVAHAGN IALRRTGGGT DHAGLGVVSL NGGFALGPAF KEDIGTSYAA
PQVAHQAARL LAEVPDASPS LLRALIGAHA RWPQACEALL NPGNNAEGRD KLLRLVGYGR
VDDAALFRSL DHTVTLLAEE RVGNDQHHFF ELPLPDSFWD GGRRTREVTV ALAYSPAVRT
TRLDYRRAKL WFHLVTAGSL DEVTQAYRRN REEGMGERAN GRWLPNDTRK NGTLQVSRWR
FKQALANGHK VFVVVTRQDS LWSDGRDGDE PYAVAVVLAD REQANAQLYA QVQAALQARA
QARARARIGG RA
//
