ID A0A1Y5JNW1_9BACL Unreviewed; 1889 AA.
AC A0A1Y5JNW1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=SLH domain-containing protein {ECO:0000259|PROSITE:PS51272};
GN ORFNames=B1748_35460 {ECO:0000313|EMBL:OUS67835.1};
OS Paenibacillus sp. MY03.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS67835.1, ECO:0000313|Proteomes:UP000195591};
RN [1] {ECO:0000313|EMBL:OUS67835.1, ECO:0000313|Proteomes:UP000195591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY03 {ECO:0000313|EMBL:OUS67835.1,
RC ECO:0000313|Proteomes:UP000195591};
RA Liu H., Cheng Y., Gu J.Y., Han W.J.;
RT "Draft genome of a polysaccharide-degrading bacterium Paenibacillus sp.
RT MY03.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000256|ARBA:ARBA00004237}.
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:OUS67835.1}.
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DR EMBL; MXQD01000088; OUS67835.1; -; Genomic_DNA.
DR OrthoDB; 222556at2; -.
DR Proteomes; UP000195591; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR Gene3D; 2.60.220.30; -; 1.
DR Gene3D; 2.60.40.1190; -; 1.
DR Gene3D; 2.60.40.3440; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR43308; OUTER MEMBRANE PROTEIN ALPHA-RELATED; 1.
DR Pfam; PF17963; Big_9; 1.
DR Pfam; PF06452; CBM9_1; 1.
DR Pfam; PF13290; CHB_HEX_C_1; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF00395; SLH; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS51272; SLH; 3.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022601};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000195591};
KW S-layer {ECO:0000256|ARBA:ARBA00022601};
KW Secreted {ECO:0000256|ARBA:ARBA00022601}.
FT DOMAIN 1704..1767
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1769..1829
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1831..1889
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
SQ SEQUENCE 1889 AA; 209836 MW; F642C4A02BA9BDB9 CRC64;
MTRVKLRRWI LAVSLIVSLL ATNLSHVRVF AADSAPEKVD YWKFERIPAG RHELSSGLNV
HQGQYALNLT FNAETEPNKF YLVKQNIPVE PNTNYTIQLW AKGDSVGKAW FGGGPGWGLR
STLVGTYDWK EFSINYKTGA SQTSFEFLIL VEGKTTNLWI DEVRMVKQGT ENNLVRNGNF
EAKSLMLSAN PPSGEVKVGT QVSLSVENQE AMIYYTTDGS DPSNSTTVKQ YEQPFAIERD
MQIKAYAKTS DGSEIEPIAF NYTTIVGEGE QLLDFDSYLE TTGKGRKVPI FKTDSLQIDG
DWEKWDAFTG IVLPSDRERQ VKMSDWKGLQ DLSAEIKFAY DDEALYIAAK VEDDIHYPVA
DSDMWVGDSL QIAFTHDSEL YGPEYGFNLF NEGRKQIWRW SDGVAKLPKE KVDYHVSRSG
TLTLYEAKLP WQAFFADKPD GKVSMTLLVN DNDGNGRKGV VEWTGAIVRG KNPKDMAELL
LLQKDEAWTV ILDGPAEYAA GFEQQYDLTI PNFGGETLTL AVTAEPFGLQ NEVIIIPGGK
VWTKKLPLTM SELGTHTLAA SAQPITGQPG KQDQLMINVL ANPQDLAAQF EQWRTKLPAL
AALLTTAEAA GLAVDYERVN YTIIDQFINY GLEDINREYY DRASYVLEEL EKLYEEASGN
VQAYISGEKM PLVVDRYVTG SIDIDKTAFV ADARSSISDE TVRKPVLFTG YGHFAQAKKD
IPLFKGYGAN MISMEIGPNS VIKPKESFTD WNIEKTGVSA QAVRDLEVGH GVSGGSLRIS
NQTPKSPGKF IDVWQEVDVE PGTAYVIKVW AKGEGVNNAW FPGGPGWGHR SPFPQGTFDW
QELTYEYKSG QNERKFRFMI ASENETQNLW IDDVRMYAKN GSGENLIVNG SFDENKFVEL
DSDDYVGDIV PIQKNVIEHL KTAEENDVAV ALLLSPHYFP TWALEKWPEL RSNNDGFIKF
TIDAPRAKQI MEDYLRLVIP LVKDYKSLHS IILSNEGVYR SYMDEANNPA WQEYLEEKYD
GDIAALNALH RTSYAKFSDV ALPDKVSRTP AFYDWVKFNN KLFSDWHRWM AGIIHEIAPD
IPLHAKIMKG AQNDIGNLTW GVDPEDFSQL SQINGNDNSN IYGRNRNFTS ELKFYDLQAS
MKEAPIFNSE HHIIVDGEER YIPEFAPHVR SVLWQGAIHG MSAATIWVWE RTYDQNSDYK
GSIMHRPDVT AAVGRTHLDL NRLADEVTAF QQDKAEAAIL YSIPAVMYDI DYPAALDNAY
EAISYNGLKV GFVSENQIEN GVLADRKTLF IPNAKHVQAS TFAALKPFVE NGGKLVIIGE
QSLTYDEYDR QLPSAERSSL LQHENTLLFP ATASSLVLRN AMTNTLEEQG LINVQLIDVD
SNELVFETEW RSVQHDGKLL INATNYTWSD KTVRVVVNGE TVTNWKNLIT GETHSEGESL
LLVAHEPVLL ELPLTGEEVE PIAHNSSFAL NLEAGTTDQH LNGTLQAEGV SNLRYEIVAN
GKLGTVELRN EATGEFVYTP HGYATGEDSF TFRVHDGNRY SNTATVTITI AASPVVNPPV
YPGATESASG QLYLPAGGAG EVSLDRQMKL TIPAGATDTS RQFAIAKLEE QKLQDLQAEN
RISPVFELSQ DPAGAFKKKV ILRIAFDAGK SGEEQKPTLM RYDVKQKMWI EVEGKVDGDS
FIAEVDQLGI YAVMVLKDEA AGPQPTKELN DIAGHWGQTW IEKAVQAGIV TGYADQTYRP
DQAVTRQELI VMLARTLTPQ AGTGQAPSFT DKETIGKWAA DAVTSAVEAG WIAGYDDGSF
RPEKGMTRVE LAAVLARVIA GTDHVGGDAG LSQFRDAEQI PLWAQSYVAR VAASGLMEGT
GAGLFKPAGI VTRAEAAAIV VRLKEQSAK
//
