ID D3EQS0_ATETH Unreviewed; 493 AA.
AC D3EQS0;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Subtilisin-like serine protease {ECO:0000313|EMBL:ADB95820.1};
GN OrderedLocusNames=UCYN_11510 {ECO:0000313|EMBL:ADB95820.1};
OS Atelocyanobacterium thalassa (isolate ALOHA).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Atelocyanobacterium;
OC Candidatus Atelocyanobacterium thalassa.
OX NCBI_TaxID=1453429 {ECO:0000313|Proteomes:UP000001405};
RN [1] {ECO:0000313|EMBL:ADB95820.1, ECO:0000313|Proteomes:UP000001405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALOHA {ECO:0000313|Proteomes:UP000001405};
RX PubMed=20173737; DOI=10.1038/nature08786;
RA Tripp H.J., Bench S.R., Turk K.A., Foster R.A., Desany B.A., Niazi F.,
RA Affourtit J.P., Zehr J.P.;
RT "Metabolic streamlining in an open-ocean nitrogen-fixing cyanobacterium.";
RL Nature 464:90-94(2010).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP001842; ADB95820.1; -; Genomic_DNA.
DR AlphaFoldDB; D3EQS0; -.
DR STRING; 1453429.UCYN_11510; -.
DR KEGG; cyu:UCYN_11510; -.
DR PATRIC; fig|713887.8.peg.1077; -.
DR HOGENOM; CLU_011263_15_4_3; -.
DR Proteomes; UP000001405; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR045986; DUF5942.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF19366; DUF5942; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ADB95820.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001405};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 427..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..389
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 403..477
FT /note="DUF5942"
FT /evidence="ECO:0000259|Pfam:PF19366"
SQ SEQUENCE 493 AA; 55460 MW; 755376BF5731D86F CRC64;
MLIKKKVKKK LLFLILFILG LSIFLVIPKK VIDQERYNSI IINFREDIPT TTLSKQIEKI
SNDYNATAIL NSVYSIDENI YIVEGGKTLL KDLKKSFLNN YTDYIEPNYV YKASKRHDDF
YQVSNVHEEW NLSNIHSDKN VGKTFERKVT IAIIDTGINK TSELQKIKFV SGYDFVNDRN
YTYDDNGHGT NIAKVITQTI NNKRVFKKVR IMPLKVLSET GEGTTSDIAD AVRFAADNGA
DIINMSLEGK SKSRILENAI NYAYNKGIII IASAGNDNHN TAYYPARYSK VISVSALDAT
GNKAFYSNFG AQVDISAPGN SNDNVNFGFN TENIIFKRSE GTGVAAAHVT GVIALIKAAN
YQKVNDIFGI LIQSSRKTNQ DPFNYFGVGQ LDSEKAIQMA FNQKITAQNF FSYLHNPNLN
FWIDNQAINY LFGTSMLITS YLFVLGLFRT CSFISSLSFN LGIVLGSSGF FFLKEFIFLT
YLNGRFVSLE VHS
//
