ID Q7NKC4_GLOVI Unreviewed; 591 AA.
AC Q7NKC4;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Glr1554 protein {ECO:0000313|EMBL:BAC89495.1};
GN OrderedLocusNames=glr1554 {ECO:0000313|EMBL:BAC89495.1};
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC89495.1, ECO:0000313|Proteomes:UP000000557};
RN [1] {ECO:0000313|EMBL:BAC89495.1, ECO:0000313|Proteomes:UP000000557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; BA000045; BAC89495.1; -; Genomic_DNA.
DR RefSeq; NP_924500.1; NC_005125.1.
DR AlphaFoldDB; Q7NKC4; -.
DR STRING; 251221.gene:10759043; -.
DR EnsemblBacteria; BAC89495; BAC89495; BAC89495.
DR KEGG; gvi:glr1554; -.
DR PATRIC; fig|251221.4.peg.1590; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_15_4_3; -.
DR InParanoid; Q7NKC4; -.
DR OrthoDB; 9798386at2; -.
DR PhylomeDB; Q7NKC4; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07484; Peptidases_S8_Thermitase_like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR045986; DUF5942.
DR InterPro; IPR017295; Pept_S8A_subtilisin_cyanobac-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 InterPro; IPR034084; Thermitase-like_dom.
DR PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR Pfam; PF19366; DUF5942; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PIRSF; PIRSF037851; Subtilisin_cyano; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000000557};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 533..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 564..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 150..403
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 419..585
FT /note="DUF5942"
FT /evidence="ECO:0000259|Pfam:PF19366"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 360
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 591 AA; 62352 MW; 9FBFC56B8916E41C CRC64;
MLSSGQSLRP RVVAMRLRKW WTALLGWMAL ALAGTAALAE PMTLPQEAVI AFRDPVSQAF
LKALQARHGV RFEANSRFSG DGRVFRVRYA PGKGAEVGAL LSQLVQSDVA EYAEPNYVYR
TLGFPNDPLY PKQWNLRAIG IESAWQKADG SGAVVAVIDT GVARRLPDMA QTDFVLGYDF
VNDDDDATDD QGHGSHVAGT IAQSTDNGEG VAGIAYRARI MPVKVLDRYG SGSALDVAEG
IKFAADNGAN VINLSLGGPG DSSVLREAVD YAHRKGVVVV CAAGNESAPQ ASYPALYANC
LSVSATGPDG SLSFFSNFGR GVDLSAPGGD KSALGADGGI LQNTIDDQGN STYASYQGTS
MAAPHVAGVA ALVYSAGVQD AAEIRKVLLS ATRPVGHDFQ NQHGAGQLNA QLALDSLENP
YWFFRGGFWW LVPLATLAVG IVLGALVMLG SRAIGFSEFF YAIGFAATGL GFFPLSAFGT
LWGPEGLLAL LATPIPNWDL RFFEGWLNPG LHTVLVPGLV AALFSGSGWG RSLAVGACVG
SAALLALQGS VFYTPLTWFT EESYARGFLL VNALLSLLLG FFVHRSGVEN P
//