ID S2YD11_9BACL Unreviewed; 1382 AA.
AC S2YD11;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Dockerin domain-containing protein {ECO:0000259|PROSITE:PS51766};
GN ORFNames=HMPREF1210_03101 {ECO:0000313|EMBL:EPD49654.1};
OS Paenisporosarcina sp. HGH0030.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae;
OC Paenisporosarcina.
OX NCBI_TaxID=1078085 {ECO:0000313|EMBL:EPD49654.1, ECO:0000313|Proteomes:UP000014412};
RN [1] {ECO:0000313|EMBL:EPD49654.1, ECO:0000313|Proteomes:UP000014412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGH0030 {ECO:0000313|EMBL:EPD49654.1,
RC ECO:0000313|Proteomes:UP000014412};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Paenisporosarcina sp. HGH0030.";
RL Submitted (MAY-2013) 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:EPD49654.1}.
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DR EMBL; AGEQ01000018; EPD49654.1; -; Genomic_DNA.
DR RefSeq; WP_016429574.1; NZ_KE150423.1.
DR STRING; 1078085.HMPREF1210_03101; -.
DR PATRIC; fig|1078085.3.peg.3071; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_004945_1_0_9; -.
DR Proteomes; UP000014412; Unassembled WGS sequence.
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; cd14254; Dockerin_II; 1.
DR CDD; cd02133; PA_C5a_like; 1.
DR CDD; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR CDD; cd08547; Type_II_cohesin; 1.
DR Gene3D; 2.60.40.4130; -; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034213; S8_Vpr-like.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 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; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
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:UP000014412};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1382
FT /note="Dockerin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004515966"
FT DOMAIN 1292..1356
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 595
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1382 AA; 150017 MW; 2968F9D807357304 CRC64;
MKRKKINKIL TGTLAVGMLL SQGAPYNVLA KSPFEPNPVE NAEEILASLS AEQRKALEQL
ETTTTFTISP DIDANSPELV KVIVEFEQAP AKIEVMKQAA KGKKLSSSAA NEKVEQSHKA
FKAHVQSLKS QKNVTNYKVE DVNITREYKK AINGVAMTLP GTAVQDLLQS GVVNRVFKDY
EVKVEPSVET QEAIDPKMAD SIPQIGVDKL HAENIKGKGI KVGVLDTGID YNHPDLKDVY
KGGYDFVDDD ADPMETTYED WINAGKPTYP GRVYFTNHGT HVAGTIAAQQ KNGVDYAVKG
VAPEVDLYAY RVLGVWGGGD TAGILAGIDQ AITDGMDVIN MSLGAATNNP LYATSVAVNN
AMLSGVVTVV AAGNAGPNEK TLGSPGTAAL GISVGASDVS MTIPTFSGSA SAEKFENMQL
LGKDFTDQLE DLQGQSLPIV FAGLGKATDF AGKDVSGKIA LIQRGEIAFD EKIKNAKNAG
AKSVIVYNNV DGQIPSYLGE VVGLIPSFRL SKADGERLKE LEEGSFTFDT LSNTKTEGDQ
LADFSSRGPV EGNYDIKPDV VAPGVSIFST TPEFINDPQD GINYDNAYVR MSGTSMASPH
VAGVAALILQ ENPEYTPFDV KSALMNTSDD LQGDNSVYEV GAGRIDAYQA VHTDTSIKVW
DKTQNIENGN IVEIDELTGS IVFGKHYKKD DQPIEASKKV TVQNIGEEEK SYTLEVEYHG
ERTGIQDAVK NGVTVDIPSS ITVGGGQVQE LQPKITIPTS AADGRYEGYI HATNTNNPDE
TYQIPFAVMV TEKGIAYLKT TRPSVTNMNP NWLNHDPIIH GIMKLNSPMK TMDVLVKDSE
TGKAVGFLGT ANMSKLLVDV DTFLVGAFAG SVYPFTNDPS KPISDYAVKL PAGDYILETI
AHDEEGGSYV THNPLIVDNT VPEVNMNIKP GVIEVNDSMY TVEDGQKAVW LHGTAKDATV
DLLQSKGLDF DQSTNTMAYY ANDTQISGYL PVEANGEVKI GIEPSDIARQ PLSLNLRTWD
IATVDDTQMY TFLKEGTEYT TSSYDKTSVK VGDNVTMTLS LNNVKQLVSG EFNLQVHNIF
KFANVKLNNS VKKYAKEKGL QVSLHEPVVK ESSSWNSLKI GASITGNAYR GLDGDMPFLD
VTFKVVNDEY YNYTPGFLVQ KSSYKKSGQT TDTAIPYYYS EYFTIISKHT QVYGNITPEA
FYISAGPGQG EYLKKADYSK IGAQVYALSR SGKKYPGTIN NKGAYTINDI PASDQEYSVV
VEIPGHLKAI QKFIPGYNEK GELRGQAIRI TQRNLAGDLN GDKMIDILDI QSVVDAYGMK
DSSIVPQDIN QDGVVDEADV RLIEKNFLTK GPDAPANKQP KEMIGKKGLE YFLRLIGLEP
KQ
//
