ID A0A268K0J8_9BACI Unreviewed; 1392 AA.
AC A0A268K0J8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 02-APR-2025, entry version 27.
DE RecName: Full=Dockerin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CHI06_15435 {ECO:0000313|EMBL:PAE40114.1};
OS Bacillus sp. 7884-1.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021693 {ECO:0000313|EMBL:PAE40114.1, ECO:0000313|Proteomes:UP000216214};
RN [1] {ECO:0000313|EMBL:PAE40114.1, ECO:0000313|Proteomes:UP000216214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7884-1 {ECO:0000313|EMBL:PAE40114.1,
RC ECO:0000313|Proteomes:UP000216214};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-2017) 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:PAE40114.1}.
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DR EMBL; NPDD01000129; PAE40114.1; -; Genomic_DNA.
DR RefSeq; WP_095249525.1; NZ_NPDD01000129.1.
DR OrthoDB; 2742965at2; -.
DR Proteomes; UP000216214; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02133; PA_C5a_like; 1.
DR CDD; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR046450; PA_dom_sf.
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; IPR050131; Peptidase_S8_subtilisin-like.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034213; S8_Vpr-like.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF65; SERINE PROTEASE APRX; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 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 Cell wall {ECO:0000256|ARBA:ARBA00022512};
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:UP000216214};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1392
FT /note="Dockerin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038663448"
FT DOMAIN 86..183
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 220..657
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 439..525
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 609
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1392 AA; 151283 MW; 5539914100FA4961 CRC64;
MRKKSYKSRI VKSLAVATIS SSFILGSIGQ VPITTKAVSY SNSENLLANL TSEQRAALHQ
LSTTETSGLQ ISSDIDLQST KQTSVIVEFA NKPAKVAKIK ASAEGQSLSE AEAAGLVQKD
HETFNQDLGQ ILTDENSKAV DYKIHHSYKH AFNGVSMSLP ANQINNLLKS KAVKSVWSNE
TFSIDPPAAD SEQLKADEAN VANYAPYDGL DRLHAEGFTG KGIKVGILDT GMDYNHPDLK
DAYKGGFDFV DDDNDPMETT YADWKKSGKP EISSGRAYYT EHGTHVAGII GGRGVADSEY
KTLGAAPEAD LFAYRVLGSY GSGSSDDIIA GIDRAVNDGM DVINMSLGNS LNDPLYATSI
AVNNAVLSGV TTVVAAGNSG DKMYTLGSPG ASALALTVGA STVAIDIYQF AGVQNGVNYS
LRQLARNYKD DLTQLKGNTY QLVDVGLGRP ADFNGKIVDK KIALIKRGSN SLIEKIKNAK
AKGAIGVLIY NDEINRAEGP IQAFVGELVD AVPSFTVTNA EGLAILAAVK AGKTDITFGD
YTKVKTSGNE LAAFSSRGPS RVNYDIKPEV VAPGASILST VPFYINDKTV DGSKPEDYKY
GYSRLSGTSM ATPYVAGVSA LLLQTNDNLE PADIKSILMN TADPLSKDYS VFEIGSGQVD
AYEAIHSNVE IQVDDRTSTL NHRNEQTIRE LTGGFSFGTI GFDDQDISEG RNIILKNRSE
KAKTFNVNVK FQTGIQGSKD AALNNVTLDA PTSVNIEGNS QHVIKFNLSI PKTAEKGTYE
GYIVFTNNED PTETYQIPFG GRVVNEGIDA FKISNPMFSA DTAWPEQAMP YMPFQFSLKS
HMKTIDVVLQ DGTTGEDLGI LGSYNGHLLP ENQLLTNTSG FNGSYYPFTG DAKNPVSSQF
VIAKTGHYKL KMVGTNNQGK TFSKEASFIY EVGAPTMTST FDSLDQKVIE YNLSQLDSNG
QFLYDFNINL KDPETEEASR LGIPVDQSNN SVVSFYNGPW PYEPIYTDKN GDYKDQILVK
QQAAPLKVQF YGMDAARNFT ADATAMLRVA FVTDTRPYYY LKANKQSIST GDTVNYSIRS
NNIKNLKTAK MTIPVIKDNG DLATIKNVVV SDAVKQYGNA EVIVTTTSDT LNTYYTITFN
YLGTKALPED MQLVNFDLQT SNIYSKGTPV NWYDMEMKGT TIDQLNVQTN NVYTYMETFK
LKPTYSRLWG SLQFEGMLNP LTGGRNNALD HRTIGAKVTV TSYDGKTVVD APLINKSGSY
VAGGMKADIN PYTVTLDVPG HFTISKSLVL SYDVRGEIIG RDMSYLLSPA KAGDVNKDHV
IDVLDAIELQ KNWGKNTSGS DLNFDGTVDK KDMDYVIKNY GLQNDSVPDA PKAKDTYKGI
TLDMVLSQLG LK
//
