ID U1GNY2_9ACTN Unreviewed; 1050 AA.
AC U1GNY2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Peptidase, S8/S53 family protein {ECO:0000313|EMBL:ERF58439.1};
GN ORFNames=H641_00547 {ECO:0000313|EMBL:ERF58439.1};
OS Cutibacterium granulosum DSM 20700.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF58439.1, ECO:0000313|Proteomes:UP000016307};
RN [1] {ECO:0000313|EMBL:ERF58439.1, ECO:0000313|Proteomes:UP000016307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF58439.1,
RC ECO:0000313|Proteomes:UP000016307};
RX PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA Brinkmann V., Meyer T.F., Bruggemann H.;
RT "Comparative genomics reveals distinct host-interacting traits of three
RT major human-associated propionibacteria.";
RL BMC Genomics 14:640-640(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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:ERF58439.1}.
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DR EMBL; AOSS01000017; ERF58439.1; -; Genomic_DNA.
DR AlphaFoldDB; U1GNY2; -.
DR PATRIC; fig|1160719.4.peg.103; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000016307; 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 CDD; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR003137; PA_domain.
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; IPR034213; S8_Vpr-like.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 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:UP000016307};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1050
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004612643"
FT DOMAIN 173..641
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 439..522
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 600
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1050 AA; 108122 MW; AA5B16D3FA0B1B56 CRC64;
MKRLTALVLT EVLLLSTPQM ASAATTQTDS ITPRPASKGG VIGTDFTPHV MNSEAETNVI
VELRKDPVAV VEARSGATMS SKQRSQLRER IKGSQKSVIS QINSSGGHVV SQMASAYNGV
HARVRGNELK KIEALPEVVA IHGAPRYKVR PTNDTSVPFL EADKVWQDVG YTGKNVKVAV
LDTGIDYTHA DFGGPGTPDA FTAASKKSDR IADPTLFGTK AAKVKGGVDL VGDKYDVSDP
KSKPHPDPNP LDCAAAGHGS HVAGTIAGLG VTTSGDTYHG PYDGTTADKK FKVGPGVAPH
ADLYAVRVFG CAGTTDVTTE AIDWAVANQM DVANLSLGGT YGTADTPDAV AARNAVASGV
IMVVAAGNEG HNPYLVGSPS TGHGVISVAA VDHAENFPGA VLTTADGHRI QAINANDAKL
ASTYNVVILK DDPATEEDES LGCSEQAYRS NGITSGANQL AVSTRGGCAR IARAVHAQKA
GAAAAAMINT DDTLPSFEGP ITGNPDTGEE YEVTIPFLGI RGPLGAKSDG DTLHGADGTT
ITLQGNSAAN SEYRHPADFT SSGPVTGTSA AHPSVGAPGV SITSVAVGSG SDGITMSGTS
MATPHVAGVA ALGVQAHPDW THQQIGQAIV TTADHDGIKG TDTHLTGTGL VDPVALVKAT
TSAHGDVTTT KLGSVADPSL SYGFVEIKDA YSTARTVKLT NHSTTTKTYR LTTQASANSD
AAEVTVSPST LTIGPGASKS AQVYLSTSVD KIGTSSDKDD QFSFHAIEGV VTATSGSERT
HVPYLLVPRA DARATVVGKP VLSKASNTIK LTKQAPAVPA TVQTFTLGAV DAKGHKETAS
DRGWDVRAIG VASAQNGSDT TLQFAINTYS NHSNAALNEY AVILDTDNNG KPDKAVFATD
SGLVNEGYAN GVTEVFIADL ATEEITPAGH LAIAPTDSST VVLPVDASTI GINGRFTYQV
ETTSGVDDEH HDRTLKATYD PNHKVFADGQ TLTIGAGQQD AELTVPFVPA AFKAAPRNGL
GLLLIAPDNA AASEALIVPK LPLRADLRNP
//