ID A0A1Q7VTB4_9ACTN Unreviewed; 958 AA.
AC A0A1Q7VTB4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase S53 domain-containing protein {ECO:0000259|PROSITE:PS51695};
GN ORFNames=AUG49_21300 {ECO:0000313|EMBL:OLE21721.1};
OS Catenulispora sp. 13_1_20CM_3_70_7.
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=1805055 {ECO:0000313|EMBL:OLE21721.1, ECO:0000313|Proteomes:UP000186605};
RN [1] {ECO:0000313|EMBL:OLE21721.1, ECO:0000313|Proteomes:UP000186605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:OLE21721.1}.
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DR EMBL; MNJN01000329; OLE21721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7VTB4; -.
DR Proteomes; UP000186605; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.12090; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR007253; Cell_wall-bd_2.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF04122; CW_binding_2; 3.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 229..641
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 97172 MW; DE9E92EAE07DBED4 CRC64;
MVAAATQAMP AQADDTQHSK HDNKMLNNAH PGWATADKDR GAVPASQRIT TRVFLTGQDP
DGLAAAARAV TDPDSPGYQQ YLTADQIKQR FGATPAQIAA VQDWLKSAGL SISAVSGDWI
DAEGDAGAVQ KAFGTQIKNY QRPDGSVGYA ASSAAVIPGS VAGLVAGVSG LSQATTRAHT
DSAQGSGITS DGDPSPGCGS TTTTYWGQYS ATGWPAGSNG STIPVLPCPY SPQQLRQAYG
LTHTGKGARI AVVDWYASKT MYSDAQQWSA DHKIQQFRDG QYTEWKNEGA WNHTSGADAC
GSAAAEESLD VEMAHGLAPD ADIVYVGANS CTDQDLMAAE QLIVDKHLAD VVSNSWGEII
HGTDGDADPA VMAGYDRIFQ KGALEGISFT FSSGDCGDDD PANKAGGAVN CNGNSARKQT
EWPVSSQWVT AVGGTTLATN SSGYAWETSM GDHRAQAQAG DASWNPGVGH IPFFFGGGGG
TSEDIVQPWY QAGKVPGALA ANVQTAAPAT RPMRVVPDVA MNGSLATSVD VAFTDGKYAH
HDMGGTSVAA PEFAAVLADV KEASGHAVGF ANPSLYALNS SAFHDVTSRS GVTEGMWSNG
DAGTLYQVGQ DTSLTATPGF DNATGLGSPA AGFEAALAAQ KGPAAPPQGG PAVTRVAGDD
RYATAIAVSK KTFPKAGSAK AVVLATGSNF PDALAGVPLA KKLGAPLLLT PGNAADPRVV
AEIHRVLAPG GKVYVLGGNA AVTPAVVSAL KVPAQRIAGD TRYTTSVAIA HALGDPSNVV
LATGNGFADA LAAGPYASDV FTSDGPAAIL LTNDRIVPPA VYDYMRDHAG VLAAVGGQAV
SAAAGTWAGH LTPLAGSDRF ETAAKVAATF PYAQNAGVAT GMQFADALTG AAMLAHENSP
LLLTMPTSLP GFTRTALQGL AHSLAGGGSV DIFGGPVAVS NAVENAVAGA VGGHVVAP
//