ID A0A1R1D4C9_9BACL Unreviewed; 3241 AA.
AC A0A1R1D4C9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OMF31801.1};
GN ORFNames=BK133_15485 {ECO:0000313|EMBL:OMF31801.1};
OS Paenibacillus sp. FSL H8-0548.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920422 {ECO:0000313|EMBL:OMF31801.1, ECO:0000313|Proteomes:UP000187405};
RN [1] {ECO:0000313|EMBL:OMF31801.1, ECO:0000313|Proteomes:UP000187405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H8-0548 {ECO:0000313|EMBL:OMF31801.1,
RC ECO:0000313|Proteomes:UP000187405};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:OMF31801.1}.
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DR EMBL; MRTK01000020; OMF31801.1; -; Genomic_DNA.
DR RefSeq; WP_076337322.1; NZ_MRTK01000020.1.
DR STRING; 1920422.BK133_15485; -.
DR Proteomes; UP000187405; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08991; GH43_HoAraf43-like; 1.
DR CDD; cd18820; GH43_LbAraf43-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.1080; -; 6.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 1.
DR InterPro; IPR010496; 3-keto-disaccharide_hydrolase.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF06439; 3keto-disac_hyd; 3.
DR Pfam; PF02368; Big_2; 6.
DR Pfam; PF16990; CBM_35; 1.
DR Pfam; PF13290; CHB_HEX_C_1; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 2.
DR Pfam; PF07691; PA14; 1.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00635; BID_2; 6.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 5.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR PROSITE; PS51820; PA14; 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:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000187405}.
FT DOMAIN 994..1137
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT DOMAIN 1544..1666
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 3058..3117
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 3118..3181
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 3184..3241
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT ACT_SITE 2255
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 2425
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 2361
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 3241 AA; 348137 MW; 4FDB53EBCC8B5BA6 CRC64;
MRNSAAGRKK SLRKALAYIL CVSMLFSFIP PAMISAAEVT STADTPLNVF HEDFNDGDSV
GWSTYESADA AFRGVWSVNA QKQYHVTNAP GAKTVADSTY FQNLVYEADL KIGGVNSDGT
GLLFRVNNLS DRVADGYTGY YAALTLDKKV TLGRVTGNGN VWKELVAPKA VGVNQGHVKI
VAVGNHIQMY LNDMTTPVID YVDNDGQQIT VGGQVGIRTW WGTSTIDNIV VREYSENKTS
APEFSVAAGN YAKSQAVSLT SATPGAVIRY TTDGSQPNSA SPVFTAPITV TSPTLIKAYA
EKTGEMVSET AEAFYSIARI EAELTDDFED GNSVGWTTYT GVQSGAWSVV NGKYEVQNAR
GDKAMLDVTP EQFVMEADIN PSASLQTSGF VFRVTDPGNG ADNMSGYFAG ISPSGSLEVG
KMNSAANNGA GKWTEITRVT AAVLPNKVNQ LKVVGLDSTY YIFVNGKLEV QFTDTEYTTG
AVGLRAWNDN NKVSYDNVKV TSLTFKAETF DENFDDGNAQ GWTTYGGTWS VTDGKYKVLD
GAGFKAVADG TNYSNLTYET DISISNATGD QNAGVLFRVS NPTVGTDNLK GYYAGIGIDG
RVSVGKFNND WTGIASIPYP ISQNKVYKMK VVAEGRNIDV YIDGEIVVSV VDRTYTEGAI
GLRTFLVDAV YDNIKVTDTG KVTQPSYDWS WVQGAVFVPT NVVNQIEQWR SYDHEINDRE
LSYAKTYGIN FVRVFMHNLL WENDKDNFIA NMNDFLALAD KYDIKVELVF FDDCWNDFPV
WGDQLAPRYG AHNSRWVEGP GDAVKANYAA NKEKLKDYVQ GVVEEFENND AVVMWNVYNE
PSNGETGLMD TVTKQIMNDS RIWIRETGSM KPMTSTGDKF SGGPFSDFIT YHPYDATYPI
YPEKFGPNSG VLADEVMNRL TQTVPGVVEN FGDKGLGFVM WEFGIGRDNT RFPWGSDVNP
LTEEPAVPFH GVVYPDGHPW DVNDIKALVG DAYDTLPIFN VQYFKDINFA QPVKKSITPR
IDFDLGNERG TGSPDPTVGI GEDNFSVRWN GTIQPAVTGD YTIYADSDNI AGVWIGGTKV
IDKKSNVREE VSGVTSLTGG DKLAVTVEYV HATGDASLHV QWSGPNMTKR VMLPVYSEIP
VESVSVTPAN VSVKVGETTQ VIASFEPVNA SNQQVIWSSS KPGIAVVSAD GVVKGITAGL
ATITATTVDG GKTATAEVNV TAGTTFTNPI VPVSSGAGSA DPSIVFKDGY YYYVKSLNDT
SLVVAKAKRL EDIGSAPRVT VYTPPAGTMY SKELWAPELQ YINGKWYIYF AADDGNNANH
RMYVLEGNSQ DPQGSYTFKG KITDSTNKWA IDGAVLQADD NSLYFLWSGW PGDVDGRQNI
YIAPMSNPWT ISGDRVLIST PTESWELNGT PRINEGPEIL KKDGKIFIVY SASGSWTDDY
TLGMLTNTDG NFLTPASWTK SGPHFTKVAT TFGPGHNTFT KSPDGTEDWI VYHATLKSGA
SWGNRSVRAQ KFTWNPDGTP NFGTPVAYNA PVEQPSGTPA VDRYKYEAED AALHGNAAVV
SSENSSGGKV VGKLDTASDY VEFTVEVADA GAYSLIVMAE NGSADSAIAE HELTVNGGTS
QSVFYQNFGW NRINPTSLDV NLNEGTNTIR LAKKTNFAQV DYIVLDRIVA DAANILPVES
LNVDKPALSI SVGTTELLTS SLKPIMVSDQ TVSVQSSNPA VATVTQVGTD SATGSAIFKV
TALVPGTAQI KVVSSANGSV MAESVVKVLP EKQEPNLSLY EVDQFDTATL NSAWSVFQEL
KSNWSLTNNN GFMTIRTTAT DIYQTTNSLN NVFLRNVPAS GDFEILAKFT APVTKNHQQA
GIIVWQNADN FVKFNHVWAD GKTLETAYEI NAKYQKPGNF VKHPGGETHT LKIKKVGNLY
TTYYWDGYEW IQASDPVTAT LSNIKVGFYA SNIVASDSPI DAKFDYFAIR EIAGGVDLSP
KTASLQVGET VQLENSGISG TAVTWTSANT NIATVSNTGL VEAKAPGRVA IQAVSNGGDF
SSKSIVTVQG DATPGEELYS EDFTSGNTAD WTTYGGVWSV KDGAYTVSSG AGYKAMLETE
QFTDFVLETD VKIVSGTEAG LVFRASNPSI GPDALDGYYV GINAAKKFAT LGMFTNGKWS
EIATRNLPID VNESYSIKVI VNENHIQVYI NDNPLNMNPY PKFDVAEPSH PSTGSIGLRT
FNAVAQFDNV KVSSYVETIT GPTYNNLNQL GGIADPHAMF YEGVYYLYGT DTANSPNMQT
GIKVYTSTDL VNWTEEGYAL RREDSWGEKQ FWAPEVIEKD GTFYMYYAVE EHLAVATSDS
PLGPFKQEVK EPIHQNPKEI DAHIFTDDDG KTYMYFVRFN NDNHLLVAEM NDDMKTIKED
TIKFVFAATQ EWENSQKAPV AKINEGPFVI KHKGTYYMTY SGNHFQSPDY GVGYATAPTP
LGPWTKYEFN PIMKANALVP GAGHHSLIQS PDGTELFMVY HTHYAIGQTE PRKLAIDRVQ
FVPQAVGPDL MEVWGPTITP QLMPSANGAI GVDSIALSGL GGATAITAKG GTLQLIATVL
PNNATNKQVT WSILDGSTFA EISANGLLKA KADGTVTVKA ESVSNPSVSN TIAIAISGQA
DVVDPEVAVE SLTISGQGGA TAITAKSGSL QLNAAALPNN ATNKDVTWSI EVGSQFATIT
AGGLLTAVAD GTVTVKAVSV SNPAVSNTIV ITISGQADVI DPEVAVESLT ISGQGGATAI
TAKAGTLQLN AAVLPNNATN KDVTWSINAG SQFATITASG LLKAVANGSV TVKAASVSNP
AVSNTIVITI SGQADVVDPG PTNPPVSTPA PEAPAKVEGN VLTLPVVKPD ASGVLTVKVA
ASDFNKLLEQ ADSKSVSIKV QNTDSAKTAV VALTAGQLEA AKAKGIESVN VDMGAATFTV
TAGQFTAGLD ASTEISLSIS KVDNSSLSAD ASAIVGSNPV YDFTLYINGA KVSDFGGETI
KVSLDYDLKS NENPNQVVVY YISDSGKPEI IKNAKYNAET GKVEFDAKHF SKYTAVNNAV
TFTDLANVAW AQTSIEALAA REIVNGVGND KFAPSSKVTR AQFITMLMNA FEFTDSSAVS
SFSDVEEGTW YYNAVALAQK LEIVKGKTDG SFGVNDEITR EEMSVMAYRA SKLAKVDLSA
AGETQQFADQ SDIAAYASES VSAMQGAGIV NGKGNNLFAP KDHASRAEAA KIIYSLFNLL
P
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