ID U9VMA7_9CYAN Unreviewed; 682 AA.
AC U9VMA7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Subtilisin-like serine protease {ECO:0000313|EMBL:ESA33760.1};
GN ORFNames=N836_20260 {ECO:0000313|EMBL:ESA33760.1};
OS Leptolyngbya sp. Heron Island J.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA33760.1, ECO:0000313|Proteomes:UP000017515};
RN [1] {ECO:0000313|EMBL:ESA33760.1, ECO:0000313|Proteomes:UP000017515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA33760.1,
RC ECO:0000313|Proteomes:UP000017515};
RX PubMed=24503993;
RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA Fromme P.;
RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL Genome Announc. 2:e01166-e01113(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC 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:ESA33760.1}.
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DR EMBL; AWNH01000094; ESA33760.1; -; Genomic_DNA.
DR RefSeq; WP_023075387.1; NZ_AWNH01000094.1.
DR AlphaFoldDB; U9VMA7; -.
DR STRING; 1385935.N836_20260; -.
DR PATRIC; fig|1385935.3.peg.5582; -.
DR eggNOG; COG1404; Bacteria.
DR OrthoDB; 543865at2; -.
DR Proteomes; UP000017515; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000017515};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 397..651
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 371
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 407
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 603
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 682 AA; 73449 MW; FCD25A7EDC50CD56 CRC64;
MVETFIEQGS DLLTGLDAFA VNAKNDLLTS GSISKHSQYF YKTDSAITDQ DAELYSLTEL
QIYEEFEAFK ESDIAHELWV SPAVTDNDLA KDLSTSFGDK PDPILGNNNS QALLSPSLEL
KDIDSSKPDV IEFSLFDASG DSTLNTIFDD GALRLNYDLG DLSSSFSSVY LEAWQEDTLT
STLGTWSEVS LSDELLNLAN FTSLTAGDYD FRLVARDGQG TNVASTSQSI SILPWLSTLG
TFGADTLTYD TFSPTGTVFL GRGGTDTLTL NGLEMGDIAN INGVSLTNFS ASNTHQAIFG
GTAFDYMTLA DGREIYFQGI EFLNFDDGSL DLLVQPRDTY FDWQWNLHIS DVSSAWRFTQ
GTEDVLLVSL DSGILTTPGT FDGVVDIDTG RLILDATDDD EFQDNGHGHQ AISVMSSAAN
NGYGVSGINW HSSVYVHDIY NSDRTPLQQA IAETIDYARR NNLKVVFQGG IQGEFWLTDG
GTQAQLEELI SANSDIAVFA IAAGNGNINI DQTSASNPSV RDGTSGGVAR LQTDHSNVIA
VGALENRHAN GNWANTWQNG LMNAGNVRRA SYSNYGESLT LMAATDSPAM DKYGNMNYFS
GTSAANPNMA GIASLVWSVN DSLDGGEVRQ ILIDTAMDLG TVGKDTAYGH GLVNADAAVR
RAWALKENQD LANLHTGSSI LA
//