ID A0A1Q6Z438_9CHLR Unreviewed; 616 AA.
AC A0A1Q6Z438;
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=AUH05_03945 {ECO:0000313|EMBL:OLB44764.1};
OS Ktedonobacter sp. 13_2_20CM_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805233 {ECO:0000313|EMBL:OLB44764.1, ECO:0000313|Proteomes:UP000185646};
RN [1] {ECO:0000313|EMBL:OLB44764.1, ECO:0000313|Proteomes:UP000185646}
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:OLB44764.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNDA01000103; OLB44764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6Z438; -.
DR Proteomes; UP000185646; 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; 3.40.50.200; 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; 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; PF00082; Peptidase_S8; 1.
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; PS51257; PROKAR_LIPOPROTEIN; 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 236..616
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT REGION 36..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 65840 MW; 786A3EBD649BD53D CRC64;
MNHKHNITLW FPLQLVLGLA IIVLLVSACS LPGAQSTTNT NATGLTPTSM PKQSTRTVAS
QPSGTGKLPS GTPLPQDEVK PLTFNLVYND AAMEQDVAQI YTPGSSTFHQ YLTSDQIVQR
YALSDVQRQQ VMNWLTQNGY TIDSTDALHT SIKVHASVAT IERTLHIKLN SYTIDNYQFF
LQQGEPKLSG PVSSLVSSVI GLDNFAFPQF QPPFGFALYT ATALSSDCGK YGTKQTLTRN
KLAAAYQVAQ LYQQGYQGEG MTIGVAEFGD SYNPQDLANY AACVGIAPPH VQNIDVDGHL
AAGTGQGEAI MDLELIAGLA PEAQILDYQT DGQSNSFAQS MVDVFNRVAE DHKVQVLSVS
YGTFESAFSS SEQAAINKSL RTLAAEGISV FISSGDCGAF TQRLPHIAAV AFPASAVYAT
AVGGTHLQVN DSNVRTSETV WSAGDNLPLC SNNWGSGGGV SENTDFKRPA WQVGTGTTTS
YDGALTHVFI RPLDFVNTIE APNGLRQVPD VAAAAYPNIA IYYKGAWVAS GGTSAAAPIW
AAGALLVDQA LQQKGKPALG GGPEFYSLAN HPGNFHPYND ITIGDNLFYS ATKGWDYTTG
WGSPNFNDIL QLELNQ
//
