ID C9ZGK7_STRSW Unreviewed; 732 AA.
AC C9ZGK7;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Putative alpha-N-acetylglucosaminidase {ECO:0000313|EMBL:CBG68977.1};
GN OrderedLocusNames=SCAB_18501 {ECO:0000313|EMBL:CBG68977.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG68977.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG68977.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG68977.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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; FN554889; CBG68977.1; -; Genomic_DNA.
DR RefSeq; WP_012999701.1; NC_013929.1.
DR AlphaFoldDB; C9ZGK7; -.
DR STRING; 680198.SCAB_18501; -.
DR CAZy; GH89; Glycoside Hydrolase Family 89.
DR GeneID; 24308928; -.
DR KEGG; scb:SCAB_18501; -.
DR eggNOG; COG3669; Bacteria.
DR HOGENOM; CLU_011988_2_1_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.120.670; N-acetyl-b-d-glucoasminidase; 1.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR007781; NAGLU.
DR InterPro; IPR024732; NAGLU_C.
DR InterPro; IPR024240; NAGLU_N.
DR InterPro; IPR024733; NAGLU_tim-barrel.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR12872; ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR12872:SF1; ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR Pfam; PF05089; NAGLU; 1.
DR Pfam; PF12972; NAGLU_C; 1.
DR Pfam; PF12971; NAGLU_N; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..732
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039507717"
FT DOMAIN 41..117
FT /note="Alpha-N-acetylglucosaminidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12971"
FT DOMAIN 132..452
FT /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT /evidence="ECO:0000259|Pfam:PF05089"
FT DOMAIN 461..725
FT /note="Alpha-N-acetylglucosaminidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12972"
SQ SEQUENCE 732 AA; 81234 MW; E6EEF3AB8E0D2AC7 CRC64;
MPLARRALLA ALAAGPAVAC APARAIPSDD TPRADRALRT ASAAARRLLP DHWRQITFAE
GREYDTFRVS GSAGRITVAG DTPATQLTGL NWYLRHIAYA EINWAGEQTD SLPRELPGLD
GAVVRRANVT HRFALNDTND GYTGAYLDWT YWERELDVLA LHGYNEVLVY AGADALYHRV
FQEFGYTEEE LRAWVPGPAH QPWWLLQNLS GFPSPVSRQL LDARAVLGRR IADRARELGM
IPVFPGYFGT VPAGFAERVP GARTVPQGRW MGFARPDWLD PRTDEFARVA AAFYRTQDEM
FGPSALYKMD LLHEGGDPGD VPVADAAKGV ERALQRAHPG ATWVMLGWQH NPPRAIVDAV
DKQHMLVVDG LSDRFPTVTD READWGGTPY AFGSIWNFGG HTALGANTPD WAALYEKWRT
KDGSTLHGIA LMPEAADNNP AAFALFSELA WREGELDLET WFAEWAHARY GARDPHAEAA
WDILRRTAYG TTRADSWSEG ADGLFGSRPA LTAVRAGRWS PKQLRYNAAD FEPALGEMLK
VRPELRASSA YRRDLLDVAR QALSNRSRVM LPQLKAAYDA KDAARLAKGS RDWLSLMDLL
DELVATDSRH LLGRWVADAR SWAVGSTERT ELAYDALSLL TVWGTREGAD AGLRDYANRE
WAGLVGGLYR LRWATYFEEL RAALAEGRAP KKIDWFALED RWARNPGTLA TEPAGDTYAV
AARVRDRLAA LA
//