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
//