ID   A0A1C1A3J9_9BACL        Unreviewed;      1513 AA.
AC   A0A1C1A3J9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=S-layer protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A8709_13595 {ECO:0000313|EMBL:OCT15137.1};
OS   Paenibacillus pectinilyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=512399 {ECO:0000313|EMBL:OCT15137.1, ECO:0000313|Proteomes:UP000093309};
RN   [1] {ECO:0000313|Proteomes:UP000093309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC13222 {ECO:0000313|Proteomes:UP000093309};
RA   Zhang J., Zhang X.;
RT   "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000256|ARBA:ARBA00037986}.
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:OCT15137.1}.
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DR   EMBL; LYPC01000014; OCT15137.1; -; Genomic_DNA.
DR   STRING; 512399.A8709_13595; -.
DR   OrthoDB; 2497113at2; -.
DR   Proteomes; UP000093309; Unassembled WGS sequence.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd15482; Sialidase_non-viral; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR001119; SLH_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR   PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR   Pfam; PF17957; Big_7; 1.
DR   Pfam; PF00395; SLH; 3.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS51272; SLH; 3.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093309};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..1513
FT                   /note="S-layer protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039097844"
FT   DOMAIN          1006..1102
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1322..1382
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          1383..1446
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          1449..1512
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   REGION          1101..1124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1513 AA;  164522 MW;  CF5342A265BF6B20 CRC64;
     MLGMKRWLMS FMVCTLALLP AAVLPVSHSA VAEQAVTGQQ PWEWHNVNLQ GMGWVTGLVT
     QKTAPYLMYA KTDVGGAYRY DRDKDEWIPL TDGFGLDQRY AYSVESINID PGHPDDVYMA
     SNGAAEVGGE IYKSTDRGAT WTPTGMASHH VYMGGNDDFR TETGERLVID PLQSEHMYFA
     SRGDGLWEKI GSLDWKQVEG GLPTVSSCVV KAGCAGATFV AFDAASGTSP TGGTKIFYVG
     VYGTGIYKTM DGGQSFALMG YPSGGEKKFN RAVVNENGNL FVSDGNTVLR AGRSDSSASK
     VLDSANFSNV NFKGIVGIDV KPDEPATLYA QASDSDAGNA WMYESVDEGA TWQAKQQMKV
     QEPAYYPSWW SNHERAGLVV DPIDPTVGWT TTGFGILKLT GINTNTPKAA ANMKGVEELV
     GYNAKVPPLA GGFDVHVGAA DSAGFSVRDR DTVPATRLMS QRYDGPPMYG INLTQMSGLD
     YSYQKPNYMA YTGYHQFSLW NGEPYHFFGT TSDGGRTWNE TAKKATLDTI GGMIAMSSTN
     PANLVWSPYN GYLKYSTDSG QTWQDASGSY SENNTHGHLY ERSSTWWSAT QNVVSDKVNG
     QKFYMFTERN ALTAEFYMST DGGKTWNLTY TGFQAKEGED FSSPNPQHLV NFAALPFTNV
     KVNPTKEGDV FLVSKPGDFP DDRATVYPKL YRSTDVSVSQ FVEVPNVQGA VDVAFGKGDL
     PDQPYIYLYG KANGDTESGV YVSKDNGATW TCITNPQQTF GRINQLEADM RYPNRVYMAL
     SGRGFVYGQL ADQPDVNVTS VTGDQALVNP IQDARVYHAG TNVTIQAAAT AKQGATIRKV
     EFFAGDRKLG EDTTAPYSLT LNQLAVGNYN IVAKATDSNG LEQFSSPQDF YVRQYSELGE
     ITYKNELGER VSDLQAGQTV EVNASLSSTS KDDHGVRLIA GLEDRSGQLV QLAQTEAKLQ
     GSGKAVYSVK IKLPAQIDGL QLKVYVSDDG YHGAVTPVST LPDTMAPTWP DTAKLYYSER
     TSHSVKLYWP DAEDGFGVAS YAVYQEGRVE PVAVLTEPAQ AHQVIINGLL PATSYHFKVV
     AQDAAGNASA PLAAADLTTK ASASGGDSTV PNQGNPTGNA ANNSGPSVVV KQKPALSNGQ
     AQVEFTLQAI QDSLNNRKDA QLILEASQVD GAKDIEVTFP SELFLPANGH EKAIIIQTQF
     ASFTLPTSFL GDKLANGQKI ELTIRPSDLT QWSGQIANKV DGRPMVDLSL RVNGDDVSHF
     QLPIQIAIPY SLRANEHANT VVGNYLTQDG KDEIIKDSYY NEAAGQLIIH VNHFSSYAVV
     VPEVTFADVK DVPWATEAID GLAVRGIIEG IGDHQFDPDR NVTRAEYVQM LVHALDFRTD
     TTVKSSFLDT QPEDWYYQAV AAAEKLGILT GYEDGSFGAN QVVTREDMAV MTARALRVAK
     LEPPMSKDNV EFKDQNQVAD YAKSDVVWLA AAGLIHGIGE NSYAPRYNTT RAQAAVLMYE
     VWKNKVRDSS VSK
//