ID A0A1Y4KXD9_9FIRM Unreviewed; 2087 AA.
AC A0A1Y4KXD9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Beta-N-acetylglucosaminidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B5F18_08515 {ECO:0000313|EMBL:OUP49273.1};
OS Lachnoclostridium sp. An181.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965575 {ECO:0000313|EMBL:OUP49273.1, ECO:0000313|Proteomes:UP000242090};
RN [1] {ECO:0000313|Proteomes:UP000242090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An181 {ECO:0000313|Proteomes:UP000242090};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP49273.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NFKJ01000012; OUP49273.1; -; Genomic_DNA.
DR OrthoDB; 9760892at2; -.
DR Proteomes; UP000242090; Unassembled WGS sequence.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 1.20.1270.90; AF1782-like; 5.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 1.20.58.460; Hyaluronidase post-catalytic domain-like; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR011496; O-GlcNAcase_cat.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR13170; O-GLCNACASE; 1.
DR PANTHER; PTHR13170:SF16; PROTEIN O-GLCNACASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 3.
DR Pfam; PF07554; FIVAR; 5.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF140657; Hyaluronidase post-catalytic domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000242090};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}.
FT DOMAIN 787..937
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 2053..2087
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 2009..2060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2009..2057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2087 AA; 229824 MW; AC389D9FBE9CF6EB CRC64;
MRKEFCMKER KRVLAAVLAA TMVCGLVPTM PPIQAEAAEQ EYELYPTPHS IEYTDGNYIL
DDSINVVYEE GVDDATKARF REVAALKELN VTESDEVVKG KTNILIGTKD NEDTYVDTYV
KKNIEQKDTD LFEKTDSYIL DSDDGVIAVL GKDNDASFYG VTTLYHVVKQ LDSFTIRNFH
VEDYADVVSR GFIEGYYGNP WSTQDRINLM KWGGYYKLNS YFYAPKDDPK HNSNWRALYT
DEEIETKIKP LAQTGNESKC RFVYALHPFM YNAIKFDKNA GYVQYQKDLA AVQAKFEQVI
KAGVRQIAIL ADDAANVGAD NYVMFLEDMT EWLQEMKKTY PDLKTTLPFC TQEYMGRGES
YYSRFPENVQ IVMTGGRIWG EVTNQFTEDF TNNAGRGPYM WINWPCTDNS KKHLIMGGYS
NFLHPGVDPD KIQGIVLNPM QQSEPSKVAI FGNASYSWNI WETEEEANQA WENSFKYVDH
NSAIENDASN ALKELSKHMI NQAMDSRVVA LEESVELKKK LTPFKESLTS GDYTTEEIED
IENEFEILQN AAKVFRAQAG DENLKDQIVY WLDCWDNTTS AALYYLEALK DYKSGDSSSL
VSNYSKGQQQ FSESKTHGFH YVDHTEYAEV GVQHIVPFIT AMETYLSKKV QEVADPTVVT
QTYISNAYNT PSVGKIENAL DGDDGTSVQF YNPNYVYKDQ YIGVEFNRPT TVNSIRFLLG
GGKNHFYYSK LQYTTDGETW KDVNGTEYSR PLNSTEPIEE NGLNLENVTA VRLIATRDNN
VDSWLLINSI DINKVEDATD KAYDVSSVSF SSEVKNAGGN VNNVVDGNKT TELWLQNSSG
ADNLPVNGAV ILDLGEEKEV GSVYIAQDTA RNNGGDILDE GVVEYSSDKQ TWKTFGELVK
ANEQTVQGDV TARYIRVRNT KQVAVWWRVS EISVFAPVRT TGKENLYTNS DDAKDFTTTV
EEKRADLSEG TITLQPEEYI GIDLKAIQKL TALDAAIEDG DVKVEASKNG VVWEELTTGD
LKDTKARYIR IINKTKKEQE IAVDKFEVTI GGIGVLGELI SSDINVISSW GDTRNDGKAF
DGDVSTATKF GGLPVKGNSA VYSFGQEIDV RSLRIYVADS QTDYIRDAKI QLSTDGKDWK
DAFEIGDGVT DTDRTTSLGG LGLGNVDTNY PNVRYFGNDA INQKASYLRI LITADYPNRA
LVMNEIMING GEYISTETNA AFEGTLEERG HKPSNMLDKD LATTYKPASE NGSMKYDISN
PEGLKTFRII QNGEASNAIV TAEFYEDGKT TNTVVGTLAQ AINEFMIPEG KTLLSVKVEW
GEKIPEISEI ITLGMEVAAT DKSELEELIA AAPDGYDSWT TSSKAEYDAV KAVAEEVNES
EYVSQETVNS AVAALKKAIS NAEVKADVSA LQALIDENLV NDNNVYTATS FSVYETAIET
AKEALENADD ISETEAAQLE SEITEAKAGL IFSIRNREIA ETTIRSYNED LAASYTTKSF
AAWTEAYEMA KALIEKDKAA EKETDRVNPT EFAAVTESYK TAEAGLVNVT TLVAAIDEFE
KTDEFLYTEE SFAVYKSAVD ESRALLLNGT KDQIKAAVDA IETAKAALVP VEEDDLQSYI
DAAKELKAAD YTEDSYAVLA DAIKEAEANI DSDNPQEWIE KLQNATKELV SVVALKEQVA
RAEGLAAEDY TTSSYGNLTQ AVEAAKELYK DGTKETVAAA VAAIENAITA LEARAEGMDE
YRDAIELKGA AGYTEDSYAA YKAAYDALMA LDSEDTSVAE FEDAKAAFEK AEAELVVAGE
AEEVSTAVLE YALKLAKDAD TTGVVESVVA RFNKAVENAQ ALLEKVQKGD ASITQEMIDE
SWKELINVMQ YLSFKQGDKE DLNKVILMAD QINLDKYLAE GKEAFTAALT EAKAVAEDGD
AMQDEVNDAW RALLKAMSEL RLKPDKSALE TLIKEAQGLD TTGSSESDVA SLTRALATAM
SVFENEEATK EEVTTAANDL EAAVRKIQAS TGETGQAGQS GTGSAATNAS GKTDKNAGNS
SQSAATNNKN AKSAKTGDMT SPAAAMAAFA LAAAAGAVAL KRKKEEE
//
