ID C9Z507_STRSW Unreviewed; 1730 AA.
AC C9Z507;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Putative secreted hydrolase {ECO:0000313|EMBL:CBG68311.1};
GN OrderedLocusNames=SCAB_11431 {ECO:0000313|EMBL:CBG68311.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG68311.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG68311.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG68311.1,
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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; CBG68311.1; -; Genomic_DNA.
DR RefSeq; WP_012999041.1; NC_013929.1.
DR STRING; 680198.SCAB_11431; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR GeneID; 24307262; -.
DR KEGG; scb:SCAB_11431; -.
DR eggNOG; COG1409; Bacteria.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG3507; Bacteria.
DR eggNOG; COG5492; Bacteria.
DR HOGENOM; CLU_252127_0_0_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08983; GH43_Bt3655-like; 1.
DR CDD; cd09004; GH43_bXyl-like; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.40.2340; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR046780; aBig_2.
DR InterPro; IPR011081; Big_4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF20578; aBig_2; 2.
DR Pfam; PF07532; Big_4; 1.
DR Pfam; PF04616; Glyco_hydro_43; 2.
DR Pfam; PF13385; Laminin_G_3; 2.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF49299; PKD domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBG68311.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..1730
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039242952"
FT DOMAIN 907..1048
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 1429..1506
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
FT DOMAIN 1517..1600
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
FT ACT_SITE 1152
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 1311
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 1264
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 1730 AA; 183950 MW; AB088C994B099D3A CRC64;
MTYIERLRGR ARRWAGPLAG LTAASLVLGL AGPAAPAAAD AAGLTDGLAL WYKLDATSGS
KAVDASGHGR DGTVNGTAGW TGNGQGLSFN GSDTYIKVPN DVMKGMDSIS VSMDVLMDEA
QTGPYFIYGF GNSSSGTGNG YLFATGNSLR TAIASGNWST EQNTRPSDGH NLSRSVWKQL
TYTQTGTTGV LYEDGAEVGR NTSVTTTPGS IGAGTTTANY IGKSVYTGDK LFQGKIRDFR
VYDRALAGSE VEQLALPIAE EGLAADKAAL TLGDTSAVTA DLTLPKTGTA GGSTITWKSD
NTGVVSNSGA VTRPAAGEPN GHATLTATLK KGPATATKSF EVTVLPTFDD TTAVKQAAEA
LTVHNLDDVR GNLTLPGDGG FGTKVAWSSA NPDVVSANGV VKRPAHGGGD TTAALTATVT
KGDAKTTRTF TAKVPELPAK EALKGYMFSY FTGEGTSDGE QLYAALSKGN DPLKWRELND
GKPVLTSTLG EKGLRDPFII RSPEGDKFYQ IATDLKIYGN GDWDASQRTG SKSIMVWEST
DLVHWTNQRL VKVSPDSAGN TWAPEAYYDD QRGEYVVFWA SKLYDNEAHS GDTYNRMMYA
TTRDFYTFSE PKVWVDRGYS VIDSTVIQHD GEYYRLSKDE RNNSSSTPNS KFIFEEKSDT
LRSLSWTAVA EGIGKGTMSA AEGPLVFKSN TEDKWYAFLD EFGGRGYIPF ETKDLDSGVW
TPSTNYDLPS KPRHGTVLPV TQSEYDRLLK TYQPDGIVTS VEDVKVTTRI GDAPVLPATV
IAEFADGAKR PVAVTWADVD PSKYAQAGTF TVKGDLPGDS AIEVRAEVTV STGGPDVPAD
LLVHYGFDEK GGSIARDSSG HGYHGTYVRT PDFATGVDGG SFKMSGGNSG SSSPYVKIPN
GVLKGADSVT VSTYAKWKGG DNWQWLFGLG PDSNKYLFAS PSNGSSSLYS AITAASWGAE
KKLSGARLTP GKWQHVTVTV DGGAKTAILY ADGVEVSRAT DVSVKPSDLY DANKDYSGYI
GRSMYSPDPY FGGEVDDFRI YDRALKPAEI LEISGNTTGI AKVTHPAQKT DAVIDDAGSR
VTLPMKPGTD LTKLAPEFTL AHGAKISPAS GTAQNFTKPV KYEVTGSDGK KRTWTVSARE
LKSPVLPGLN ADPNIVRFGD TFYIYPTTDG FEGWSGTQFK AYSSKDLVNW KDHGVILDLG
PDVSWADSRA WAPAMEERDG KYYFYFCADA NIGVAVSDSP TGPFKDALGK PLLKAGTLPG
QMIDPAVFTD DDGKSYLYWG NGRAYVVPLN DDMVSFDSAK ISDITPSGYN EGTFVIKRKG
TYYFMWSEND TRDENYQVAY ATGSSPTGPW TKRGVILEKD LSLGVKGPGH HSVVHVPGTD
DWYIAYHRFA IPGGDGTHRE TTIDKLEFDA DGLLKKVVPT LESIDPVTIA RAGADVSGKE
GSKIQLNGTV SGAGTAKWTA EKGAPCVFAD AGSARTTITC ADNGTYEVTL TGGRSSDTAT
VTVTNAAPEI TSVSSGKTVE TGKVTRVRVK FTDAGTRDEH TCRIDWKDGS KPAAGKVTAG
SCKAEHTYRT AGLFAPVITV TDDDGASVSH TVAELVVYDR KAGGATGDGS FTSPAGAYPA
GPKLTGKADF SFTAAYGKSG NKPSGKVAFD FAGAKLKFRS TSTEWLVVTG SEAVLQGYGT
VNGKGGYLFR VTATDGPDTF QIKIWKKSDG KVVYDNRTAS TTKGVTIGRK
//
