SLAP2_ACET2
ID SLAP2_ACET2 Reviewed; 688 AA.
AC Q06853; A3DJZ6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cell surface glycoprotein 2;
DE AltName: Full=S-layer protein 2;
DE Flags: Precursor;
GN OrderedLocusNames=Cthe_3079;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8458832; DOI=10.1128/jb.175.7.1891-1899.1993;
RA Fujino T., Beguin P., Aubert J.-P.;
RT "Organization of a Clostridium thermocellum gene cluster encoding the
RT cellulosomal scaffolding protein CipA and a protein possibly involved in
RT attachment of the cellulosome to the cell surface.";
RL J. Bacteriol. 175:1891-1899(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Assembled into mono-layered crystalline arrays.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer.
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DR EMBL; X67506; CAA47842.1; -; Genomic_DNA.
DR EMBL; CP000568; ABN54275.1; -; Genomic_DNA.
DR PIR; T18263; T18263.
DR RefSeq; WP_003519375.1; NC_009012.1.
DR PDB; 5G5D; X-ray; 3.00 A; A=205-364.
DR PDB; 5K39; X-ray; 1.98 A; A=205-364.
DR PDBsum; 5G5D; -.
DR PDBsum; 5K39; -.
DR AlphaFoldDB; Q06853; -.
DR SMR; Q06853; -.
DR STRING; 203119.Cthe_3079; -.
DR EnsemblBacteria; ABN54275; ABN54275; Cthe_3079.
DR KEGG; cth:Cthe_3079; -.
DR eggNOG; COG1361; Bacteria.
DR HOGENOM; CLU_399939_0_0_9; -.
DR OMA; IFANIKF; -.
DR OrthoDB; 12506at2; -.
DR BioCyc; MetaCyc:MON-16410; -.
DR Proteomes; UP000002145; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002102; Cohesin_dom.
DR InterPro; IPR001119; SLH_dom.
DR Pfam; PF00963; Cohesin; 2.
DR Pfam; PF00395; SLH; 3.
DR SUPFAM; SSF49384; SSF49384; 2.
DR PROSITE; PS51272; SLH; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Reference proteome; Repeat; S-layer; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..688
FT /note="Cell surface glycoprotein 2"
FT /id="PRO_0000032635"
FT DOMAIN 36..201
FT /note="Cohesin 1"
FT DOMAIN 207..370
FT /note="Cohesin 2"
FT DOMAIN 453..520
FT /note="SLH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DOMAIN 521..584
FT /note="SLH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DOMAIN 585..648
FT /note="SLH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DOMAIN 649..669
FT /note="SLH 4; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT REGION 372..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:5K39"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:5K39"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:5K39"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:5K39"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:5K39"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:5K39"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:5K39"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:5K39"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:5K39"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:5K39"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:5K39"
FT STRAND 312..322
FT /evidence="ECO:0007829|PDB:5K39"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:5K39"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:5K39"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5K39"
SQ SEQUENCE 688 AA; 74971 MW; 8E2BD2BADBD5D2FF CRC64;
MKKNNVLTIA AMIALLLTSL LTSITFGETS SIPSRISMEL DKTKANIGDI IIATIRIDNI
NNFSGYQLNI KYDPSYLQAV NPLTGEPIKK RTMPAVNGTV LLKGDQYSIT EVVENNVDEG
ILNFGKGYAN LTEYRKSGKP ETTGIIGKIG FKALKLGKTE IKFENTPVMP GAKEGTLLFD
WDAETITEYN VIQPKELAIT LPDDAHIALE LDKTKVKVGD VIVATVKAKN MTSMAGIQVN
IKYDPEVLQA IDPATGKPFT KETLLVDPEL LSNREYNPLL TAVNDINSGI INYASCYVYW
DSYRESGVSE STGIIGKVGF KVLKAANTTV KLEETRFTPN SIDGTLVIDW YGQQIVGYKV
IQPDKITVIS EPEVPTQTPT QTPPTTTAPS QTPTQTPPTT TAPSQTPTQT PAVTPTQSAT
PSDPGGGGGG LPGGGGGAVN PSASPTPTPT SKPTPTATKK PEPTEIEEPE PEIPGTVGIH
YSYLTGYPDK MFRPEKSITR AEAAVIFAKL LGANENTKIN YNVSYTDVDS SHWASWAIKF
VSYKKLFTGY PDGSFKPNQN ITRAEFSTVV FKLLVSEKGL KEEKIEKSKF GDTKGHWAQQ
FIEQLSDLGY INGYPDGTFK PNNNIKRSES VALINRAMGR GPLHGAPQVF EDVPQTHWAF
KDIAEGVLNH RYKLDNEGKE QLLEIIDN
