ID   A9KRL2_LACP7            Unreviewed;       951 AA.
AC   A9KRL2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   04-NOV-2026, entry version 90.
DE   SubName: Full=Glycoside hydrolase family 85 {ECO:0000313|EMBL:ABX42086.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Cphy_1714 {ECO:0000313|EMBL:ABX42086.1};
OS   Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS   (Clostridium phytofermentans).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC   Lachnospiraceae.
OX   NCBI_TaxID=357809 {ECO:0000313|EMBL:ABX42086.1, ECO:0000313|Proteomes:UP000000370};
RN   [1] {ECO:0000313|Proteomes:UP000000370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700394 / DSM 18823 / ISDg
RC   {ECO:0000313|Proteomes:UP000000370};
RA   Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA   LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT   "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00081}.
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DR   EMBL; CP000885; ABX42086.1; -; Genomic_DNA.
DR   RefSeq; WP_012199740.1; NC_010001.1.
DR   AlphaFoldDB; A9KRL2; -.
DR   STRING; 357809.Cphy_1714; -.
DR   KEGG; cpy:Cphy_1714; -.
DR   eggNOG; COG3291; Bacteria.
DR   eggNOG; COG4724; Bacteria.
DR   HOGENOM; CLU_008357_0_0_9; -.
DR   OMA; AADDRFW; -.
DR   Proteomes; UP000000370; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:InterPro.
DR   CDD; cd06547; GH85_ENGase; 1.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR054110; EndoD-like_D2.
DR   InterPro; IPR032979; ENGase.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR005201; TIM_ENGase.
DR   PANTHER; PTHR13246:SF1; CYTOSOLIC ENDO-BETA-N-ACETYLGLUCOSAMINIDASE; 1.
DR   PANTHER; PTHR13246; ENDO BETA N-ACETYLGLUCOSAMINIDASE; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF21910; GH85_C; 1.
DR   Pfam; PF03644; Glyco_hydro_85; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS50093; PKD; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000313|EMBL:ABX42086.1};
KW   Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000370};
KW   Signal {ECO:0000256|PROSITE-ProRule:PRU00303, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..951
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303,
FT                   ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5049024026"
FT   DOMAIN          724..794
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          804..949
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   951 AA;  105902 MW;  103A4C84C0C92DBB CRC64;
     MKKQYYKFVS VALIATMFVT GCSKNSSDIK DNATNSEAVV TEAVQVPEKE QAPEENQAPG
     KIVYRVTPES ESDMKMMNIP NAPYWFPAEL LEWNPKEAKD LDLYVSNVPL KSRVDKSKLV
     KSNKTQIADF KVAALSIMNS RTSGNSPHGL NRFNANTFSY WQYVDQLVYW GGSAGEGLIV
     PPTADVTEAA HTNGVPVLGT IFLAPEAWGG KIVWLDDFLK TDENGQFLLV DKLIEVCTVL
     GFDGWFINQE MGGTKEAPLT KEHADKMLSF VQQFNEKSAG KFSFIWYDSM TEEGEIDYQN
     ALTDKNDAFL VDGNGKKGAD SMFLNFWWAA RELADQELLV KSNEKAKEKG INPYDLYAGI
     DVQANGVMTR INWDLFEKNN VPHTSIGLYC PSWTYFAADS LDAFERYENR MWVNEHGNPT
     IPTEVSQYDW HGISTYAIEK TVVNQLPFIT NFNKGNGYNF FVNGEKISLQ DWNNRSITDV
     MPTYRWILNQ EEGNKLKPGI DYADAYYGGN SIRLYGAMET DKKSELTLYS SDLAIGDKTK
     AYAMLKANYK VNAELVLELE DGSKEYIKGD NTLNTEWAKI VFDLSKVKGK TVKKIGFNFT
     SSKSDMILIN MGNLTIFEEN TVAPTTPGNL KIAYQQFDDD GLFAGVKLAW DGASNVRYYE
     VYKINDDGSK SFQGATTAKA HYMNALVREE GEKKSTFEVI AVNNMQQRSQ GTTVVMEWPN
     ISLPKANMKA SKTLVAPGEV VEFTSLCSQN TTGYEWSFEG ADHAASTEQN PKVTYSKEGV
     YNVSLVAKNG EGTAEYKVDG LIVVRSDASG DIPVVSEGKT TSASGYVNEN EAPRFAVDGK
     TNTKWCATGS APHDITIDLG ENKMVSEVYM AHAEKGNESS DMNTSWYTIE TSLDGKSFEP
     AIEVKNNASA ETLDAFKPRE ARYVKVTVMK PTQGSDTAVR IYEIQVHGLD K
//