ID F2JRK0_CELLD Unreviewed; 1472 AA.
AC F2JRK0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Cellulose-binding family II {ECO:0000313|EMBL:ADZ83921.1};
GN OrderedLocusNames=Clole_2208 {ECO:0000313|EMBL:ADZ83921.1};
OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS RHM5) (Clostridium lentocellum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ83921.1, ECO:0000313|Proteomes:UP000008467};
RN [1] {ECO:0000313|EMBL:ADZ83921.1, ECO:0000313|Proteomes:UP000008467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC {ECO:0000313|Proteomes:UP000008467};
RX PubMed=21398547; DOI=10.1128/JB.00239-11;
RG US DOE Joint Genome Institute;
RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA Angert E.R., Currie C.R.;
RT "Complete genome sequence of the cellulose-degrading bacterium
RT Cellulosilyticum lentocellum.";
RL J. Bacteriol. 193:2357-2358(2011).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; CP002582; ADZ83921.1; -; Genomic_DNA.
DR RefSeq; WP_013657215.1; NC_015275.1.
DR STRING; 642492.Clole_2208; -.
DR KEGG; cle:Clole_2208; -.
DR eggNOG; COG1800; Bacteria.
DR eggNOG; COG4305; Bacteria.
DR HOGENOM; CLU_250122_0_0_9; -.
DR Proteomes; UP000008467; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.290; -; 2.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR027797; PT-TG_dom.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR37467; EXPORTED CALCIUM-BINDING GLYCOPROTEIN-RELATED; 1.
DR PANTHER; PTHR37467:SF1; EXPORTED CALCIUM-BINDING GLYCOPROTEIN-RELATED; 1.
DR Pfam; PF00553; CBM_2; 2.
DR Pfam; PF14449; PT-TG; 1.
DR Pfam; PF18884; TSP3_bac; 5.
DR SMART; SM00637; CBD_II; 2.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS51173; CBM2; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50234; VWFA; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1472
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003280533"
FT DOMAIN 44..165
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 162..272
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 718..873
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
SQ SEQUENCE 1472 AA; 163719 MW; F6402E9BD2F8772F CRC64;
MKTKKRILAY LLTLTLAMTS LPTQLFAQTT KDVPLPMSAL VDTQTTTPGA IQINPSKYIG
DGYQVEFKVT NQWPGAFNGE FVLTNTGDKP LENWTLKFDF EHEITSMWNA QILTRESNSY
AIKNMGWNQD IEPGSSITIG FQANGDGTIN NPSKYSLNME EQVASDVDYT IGFKLTGNWN
GGFNGEISIT NQSNAPIEDW SLAFDFEANI NNLWTATIVE HTGNHYVIKN KGYNANIAPG
QTLTLGFSGD NLEDSTIEPN NYKLSYIGSA TDKEEIDYEL DSDNDDLPDY YENILGTDPL
NADTDGDGLP DGYEYCELMT DPLLQDSDGN NTSDADEDFD KDGLINREEF LLSTDPYNND
TDKDSLLDGD EVNKFGTDPL VYDEIDIRID TDGDGLADQT ERIIGTDLTK IDTDNDGLPD
NYEYFDFITN PTLSDTDNNG INDADEDFDN DGLTNLEEYT IRTDSFKPDS DNDGLIDGDE
VNTYHTNPLI ADTDGDTLND GDEISMGLDP LNPFTFGTPD QEYVFVQDVA DDNLSAINTE
DSPYKVSIQV KASGNAKGNT IVGQSEYAHT IEDNNAIVGK AISIKYHDGV LEEGKISFEL
DESLVTQDNI VNDQRVTGIK RYQIFNFNEE YGILVPLPTI VDVKTNVIST EMIGQGTYCV
MNLEKWLSNV GAFKTNQEVN ILKQSASIMA SVDTQTYDLK NNNLFNTTYP NTKSKKVDLA
FVIDTGYTMQ KIMPSLKASM KEIVRGLKEE YNLDVEVSII DFKDINYMSP SSAIQINGIQ
ASKAEGNRVL SFSNSLSEIE QIIDGLDAYG GYDTDISGTP LAGLGYVTTL PFRKDASKFA
FLVTDKSYSI ANCHGFNTVY EMIEKLNTSG VNLGISYKTR EETGSISDNT ATFYRRWLQK
INGVFVPLRI MADVESGFKE FIITNLIDQK EFQILGSTSL KEIILKEPLA KGGSADTDKD
QLTDSEEVYW DSKLISYGID GYELPKIGDI WTLIYETHGY DISQIPFPEL LQDIVVLPIL
SDPTDIDSDS DGLTDYVEHT NHFEHDTWSA LHYDKTNVDI YNTYERTVAH SKDEHTFILN
PYIVTRPYTI NVNSDINLDI SVYYIGITGM SDPELVTTKY NIQDRIDFVP EKGGYYEVRI
KLSSITSIGD YSMTIELLDM YKEAGFVEGD DVLVYAANHK GLYPFLATLE EGTYGILIPK
FEDAEEFGQF NCAFSPGDGL SLVLDLTPLI GDAKTFIELI EGRDIITKQE INRWLLAGAI
IVPRVVSEAI GLFGKNADDV AKYILKGDPK TVAKLKELGA TDGLITSIQK SEGAAGLDRL
EKLLMQYFSC DDIATLSKYG ISTAEYQAKG ITYSSVAENV SKMLNTSDSY VELYRAVGVD
EFEDIMSSNI FRPSPSGFVS KQFGFSFDEI LKLSNNFPES VAIFKAKIPK EVFIKLDFNA
VDTAILKSGN ATVQEDVLKI FNDSLLEVKQ VY
//