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Database: UniProt
Entry: R7GEF5_9CLOT
LinkDB: R7GEF5_9CLOT
Original site: R7GEF5_9CLOT 
ID   R7GEF5_9CLOT            Unreviewed;       247 AA.
AC   R7GEF5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Endo-1 4-beta-xylanase B (Xylanase B) (1 4-beta-D-xylanxylanohydrolase B) {ECO:0000313|EMBL:CDE25396.1};
GN   ORFNames=BN598_00203 {ECO:0000313|EMBL:CDE25396.1};
OS   Clostridium sp. CAG:307.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262795 {ECO:0000313|EMBL:CDE25396.1, ECO:0000313|Proteomes:UP000018128};
RN   [1] {ECO:0000313|EMBL:CDE25396.1, ECO:0000313|Proteomes:UP000018128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:307 {ECO:0000313|Proteomes:UP000018128};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDE25396.1}.
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DR   EMBL; CBIO010000057; CDE25396.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7GEF5; -.
DR   Proteomes; UP000018128; Unassembled WGS sequence.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   PANTHER; PTHR48081:SF6; PEPTIDASE S9 PROLYL OLIGOPEPTIDASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000313|EMBL:CDE25396.1};
KW   Glycosidase {ECO:0000313|EMBL:CDE25396.1};
KW   Hydrolase {ECO:0000313|EMBL:CDE25396.1};
KW   Polysaccharide degradation {ECO:0000313|EMBL:CDE25396.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018128};
KW   Xylan degradation {ECO:0000313|EMBL:CDE25396.1}.
FT   DOMAIN          86..234
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   247 AA;  28392 MW;  98811896CCAB2CF6 CRC64;
     MEKIMLDDAN YYTTCYKDDK KRHMVVIAPG GGYDHTSLLE AFNVASKFNE NGFHASVLNY
     RETLDSYPYP QKLLAKTISE LRRDSRNDKI ISIGFSAGGH LALSNALFYN EYGFCSKPDY
     LILCYPVISS NYHIWHQGSF KALLGDNYNE ENLEKMSLER HITSDLCPIF IWHSITDESV
     SVLNSIELLQ ALKAKKVKAE CHIFQEGVHG MSLSDETTGI KDKRKENPYV ARWFSMMLEW
     LNHNLNE
//
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