ID A0A2S4Y9U6_9ACTN Unreviewed; 327 AA.
AC A0A2S4Y9U6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Chitin-binding protein {ECO:0000313|EMBL:POX45717.1};
GN ORFNames=C3489_33605 {ECO:0000313|EMBL:POX45717.1};
OS Streptomyces sp. Ru71.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080746 {ECO:0000313|EMBL:POX45717.1, ECO:0000313|Proteomes:UP000237414};
RN [1] {ECO:0000313|EMBL:POX45717.1, ECO:0000313|Proteomes:UP000237414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru71 {ECO:0000313|EMBL:POX45717.1,
RC ECO:0000313|Proteomes:UP000237414};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-2018) 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:POX45717.1}.
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DR EMBL; PQSS01000094; POX45717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4Y9U6; -.
DR OrthoDB; 5179374at2; -.
DR Proteomes; UP000237414; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd21177; LPMO_AA10; 1.
DR Gene3D; 2.70.50.50; chitin-binding protein cbp21; 1.
DR InterPro; IPR004302; Cellulose/chitin-bd_N.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR019931; LPXTG_anchor.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; NF041528; strep_LAETG; 1.
DR PANTHER; PTHR34823:SF1; CHITIN-BINDING TYPE-4 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34823; GLCNAC-BINDING PROTEIN A; 1.
DR Pfam; PF03067; LPMO_10; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000237414};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..327
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015540178"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 288..327
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 213..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 33537 MW; ED5F79E8BC6DC2C1 CRC64;
MPARRTAATA AVLGLAPLAL TALAAAPAAA HGTMGDPVSR VSQCYAEGPE SPKSAACKAA
VAAGGTQALY DWNGIRIGDA AGRHRQLIPD GKLCSANNEE FKGLDLARAD WPTTDVHSGS
YTFRYRVTAP HKGTFTVYAT KPGYDPARPL AWSDLDLAHP VATALDPVAA GGFYTFTGTL
PERSGRHLLY AVWQRSDSPE AFYSCSDVSF GDSATHSAGT SPAPSAPSAS APSEEQIEAG
AGRSTIEHHG HGDADASTSA EPRSAGRPDA ARTAQGNRVR AAGAGERLAE TGGDGSTPYL
ALGGAAALAI GAAALFASVR RRATVRR
//