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Database: UniProt
Entry: A0A1F5G2H6_9BACT
LinkDB: A0A1F5G2H6_9BACT
Original site: A0A1F5G2H6_9BACT 
ID   A0A1F5G2H6_9BACT        Unreviewed;       594 AA.
AC   A0A1F5G2H6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Dockerin domain-containing protein {ECO:0000259|PROSITE:PS51766};
GN   ORFNames=A2696_04100 {ECO:0000313|EMBL:OGD86035.1};
OS   Candidatus Curtissbacteria bacterium RIFCSPHIGHO2_01_FULL_41_13.
OC   Bacteria; Candidatus Curtissbacteria.
OX   NCBI_TaxID=1797745 {ECO:0000313|EMBL:OGD86035.1, ECO:0000313|Proteomes:UP000177069};
RN   [1] {ECO:0000313|EMBL:OGD86035.1, ECO:0000313|Proteomes:UP000177069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:OGD86035.1}.
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DR   EMBL; MFBA01000006; OGD86035.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5G2H6; -.
DR   Proteomes; UP000177069; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; cd14256; Dockerin_I; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 2.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..146
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000259|PROSITE:PS51766"
FT   ACT_SITE        271
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        312
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        480
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   594 AA;  65342 MW;  2D546F186CB2084E CRC64;
     MLNKTIKVKA LEFGKLAKYL LIIGIVAFGL IYLLIDNTKT SQAATDQTIT DQNGDGIINL
     VDARILAPPA VTNCPVCVDV NSDRTINQKD FDLVQSYIDQ NAKLLEAGAP EASYKPRFDI
     NADGKIDTDD MVIIKNYFGQ VAQEPVFGLG NPQELTFGFM ANDILIKFKP GTTDSQKQTI
     FTKYNLSKKR SFDQINTTNL ATPDVNVENL QKQLAQEPVV QSTTKNYLGE WATDDPYWDD
     QWGHQKIRIE QTWYTETQGR TPNKVRVAVI DTGADYSHYD LGQNLSQTLR RNVEIDPSWG
     FEQQDVTDEN GHGTFMAGII GATANNGQGI AGLNWNVEII PIKIPTNVYG QPILSWIYVA
     LEWTAMNHED IDVVNMSFGF PDRTSDENMD YYLNALDSFG VILVAAAGNL GRDDSEYPAN
     HPKVVSVGAT LANDLLCPDS SGRTSADIFA PGDYIFSTVP IELDWIGPQD GVAYYGCGTS
     AAAAYVSGVA ALCRVVAPVS PSRDDLKCNK FEHNGFGRID AWASVWYKNC SRFDFNGNGE
     IGVIDARRLA RAYNTSSGDP LYNVLYDIAP VGTDGQISIA DALLILNRQG FTCQ
//
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