GenomeNet

Database: UniProt
Entry: A0A089X507_STRGA
LinkDB: A0A089X507_STRGA
Original site: A0A089X507_STRGA 
ID   A0A089X507_STRGA        Unreviewed;      1208 AA.
AC   A0A089X507;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Secreted peptidase {ECO:0000313|EMBL:AIR98248.1};
GN   ORFNames=SGLAU_11220 {ECO:0000313|EMBL:AIR98248.1};
OS   Streptomyces glaucescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1907 {ECO:0000313|EMBL:AIR98248.1, ECO:0000313|Proteomes:UP000029482};
RN   [1] {ECO:0000313|Proteomes:UP000029482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX   PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA   Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA   Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT   GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT   plasmid.";
RL   J. Biotechnol. 194:81-83(2015).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; CP009438; AIR98248.1; -; Genomic_DNA.
DR   RefSeq; WP_043500649.1; NZ_CP009438.1.
DR   AlphaFoldDB; A0A089X507; -.
DR   STRING; 1907.SGLAU_11220; -.
DR   KEGG; sgu:SGLAU_11220; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_007528_0_0_11; -.
DR   OMA; EYRTVWR; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000029482; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.30.30; -; 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; 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; IPR017296; Peptidase_S8A_SAM-P45.
DR   PANTHER; PTHR43806:SF59; EXTRACELLULAR PROTEASE; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PIRSF; PIRSF037852; Subtilisin_rel_SAV5721; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 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};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000029482};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1208
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039344873"
FT   DOMAIN          215..474
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        224
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        256
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        429
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1208 AA;  124454 MW;  14D2301343129EB2 CRC64;
     MIRGPVGRGA ALLSAGLVLP LLPAAQADAA DAAGGTAAAP AVTRTASAAR TVTLVTGDRV
     TVTDLGGGRK AVEVERPAGA TGAVRTRGAN GALSVVPDEA LPYLRAGTLD ERLFDVGALL
     RQGLGDDRSD ALPLIVTYEK GARAVTPRGA ARTRALPSVR GAAVAAGRGR VFWREFTRPG
     TGIDRVWLDG RVTADMAESN AQIGTPAAWQ AGLTGEGVTV AVLDSGVDAS HPDLAGRITA
     SRSFVEGEEI ADRNGHGTHV ASTVGGSGAA SGGTERGVAP GADLAVGKVL GDQGSGSESQ
     IIAGMEWAAR EVGADIVSMS LGSTEPSDGT DPMAQAVNTL SAQTGALFVV AAGNTGAPSS
     IGSPGAADAA LTVGAVDAAD TAAPFTSAGP RHGDHALKPD LAAPGVGILA ARSSLSEGSG
     AYTAMSGTSM AVPHVAGAAA LLAERHPEWT GARLKDALLS TSAPLDASAY TLGAGRVSVP
     DAVRARVTAT GSVDFGFFRW PYEANEPVTR TVTYANSGDE PVTLELSVRG ADGVATLADA
     TLTVPAHGTA STTVTGDGAR APAGNTSGRI VAAVAGTPVA HTVFGLVKEE ERYTLTVHVK
     DRDGAGDAAD LVVQRLAATA EPVPAHVGAS GTLRLRLAPG TYSVTSFLDV RGGHGADSLG
     LGFLADPEIV LDRDREVTLD GRRLRQITAE VGRRTQTRQL LMEYDRRAHG AELFGAVMVP
     VTYDSVFAAP TRKVTRGSFE YRTVWRLGKP PLAVRGVGEA LAQSGGTLAE GRVRLPLADV
     GRGPLTGVRG KAVLAELTEG TEPAALAAAA EDAGVAALFV TDDAPGRLNA WWGSDDGGDR
     PFPIATVGAA DARRLRDAGR VDMTGTKNTP YVYDLSKGYP GAVPDRDLTY RPGRELAAVR
     AGFHAARPVS GAEFRYSITG TFPIGVGFKE RIDYPAERTD HVSTGPGQLW HESVDLGAGE
     LEQRSGLVRY RGGTRPALDW FKPVWHPWLG TGLGWGQERT GGRLSFNTPG WGDSGPDHTG
     FGDVWSEESG MSQTTAVYLD GELVDRRTGS TAYVGDAPAE ERTYTVVTDT ALDPARWPAA
     TEGHTEWTFR SAGTPEDRRT VLPLINLGFG LGTDLAGTVP EGRLPVRVHA EYVRGAAGTG
     TLGGGTLDVS YDEGVTWREV PLGEAGPAAW RGTLHVPEGA ASVSLRASAR DDRGGSVVQE
     IVRAVTVR
//
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