ID A0A1Q8Q9U6_9BACI Unreviewed; 859 AA.
AC A0A1Q8Q9U6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=BIG2 domain-containing protein {ECO:0000259|SMART:SM00635};
GN ORFNames=BTO30_01470 {ECO:0000313|EMBL:OLN24110.1};
OS Domibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714264 {ECO:0000313|EMBL:OLN24110.1, ECO:0000313|Proteomes:UP000185568};
RN [1] {ECO:0000313|EMBL:OLN24110.1, ECO:0000313|Proteomes:UP000185568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XD80 {ECO:0000313|EMBL:OLN24110.1,
RC ECO:0000313|Proteomes:UP000185568};
RA Verma A., Krishnamurthi S.;
RT "Domibacillus antri genome sequencing.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:OLN24110.1}.
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DR EMBL; MSDU01000003; OLN24110.1; -; Genomic_DNA.
DR RefSeq; WP_075396928.1; NZ_MSDU01000003.1.
DR AlphaFoldDB; A0A1Q8Q9U6; -.
DR STRING; 1714264.BTO30_01470; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000185568; 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 Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.40.1080; -; 2.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF02368; Big_2; 2.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00635; BID_2; 2.
DR SUPFAM; SSF89260; Collagen-binding domain; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 2.
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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..859
FT /note="BIG2 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039070700"
FT DOMAIN 608..679
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 681..749
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT REGION 431..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 350
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 859 AA; 92575 MW; 2965E79338468518 CRC64;
MSVLKLVKCV LAVFLVLGSL NLISAEGAAN DAKTREREDK LAQEKEKQIL IQYKESSKKS
EYAAKKKLYS ASISAIEPIA PLTEVITVKD KKNVDALIKE LKKDNSVQIV EKNRISHVSA
LTNDPYISSQ WWLDTVNAVP AWPHTDQQRK QIVTAVIDSG LDTSHVDLKN KIARGGYDFY
SGTAVMSDPN GHGTKVSGVM AAEANNAAGI AGVTGEFDVK ILPLRVANYE GESYVSDVIE
AIDYAISMNV DVINISLGSD SSSSLENAAI QRAADAGIII VASAGNEALE GNPILYPASY
ENVISVGAVD QYKNRSSFSN YNSYVDVTAP GEEVYTTAPY QSYEYVNGTS FSAPIAAGIL
SIAKALKPEL TVDEASDLIE TTADDLGTAG YDIQYGHGLV NAGRVVTTLL ADSAASVTGV
QLDKSTVNMS FSSPTSSASN TAETKKQQMN EATKTKTAIM DETRLVNELD LYESEPNDDT
SSANNISLNS YLSGSITDYY FDTDYYRFTV DQPGTFTIDA AWVSGYVAGY GYEDDLEVVL
LDENGDIMTY ADYQPFSDGT ASRFMSRHID AGTYYITVFQ SSDYQSLYTD EWYGISAMFE
ADQSSEQPAP VISLTTDTLF LKKGQSDSLL QAGNSITAIQ WSSSNPAAAA VDQNGNVTGT
GYGKAVISAA ANGKTIQCVV KVTADTVNPT AALFETVLPA DARNKNVTWK SSNPSVATVD
QYGIITAKGQ GTAVITVITD EGNFRASSTV NVTGSKTTWT DFSAKDVKTD KVFTVQFNFP
VDPQSVNSTN IYVAADKDGI NRIPEAQVYV NAENNQLIHI APGISWPPGT YYLFVTNQLK
STDGKTHNKN IRMPFTVTN
//
