CSG_METAC
ID CSG_METAC Reviewed; 671 AA.
AC Q8TSG7;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Major S-layer protein {ECO:0000305};
DE AltName: Full=Cell surface glycoprotein {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=MA_0829 {ECO:0000312|EMBL:AAM04268.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, SIGNAL PEPTIDE, FUNCTION, SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION.
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=19228054; DOI=10.1021/pr800923e;
RA Francoleon D.R., Boontheung P., Yang Y., Kin U., Ytterberg A.J.,
RA Denny P.A., Denny P.C., Loo J.A., Gunsalus R.P., Loo R.R.;
RT "S-layer, surface-accessible, and concanavalin A binding proteins of
RT Methanosarcina acetivorans and Methanosarcina mazei.";
RL J. Proteome Res. 8:1972-1982(2009).
RN [3] {ECO:0007744|PDB:3U2G, ECO:0007744|PDB:3U2H}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 318-594.
RX PubMed=22753492; DOI=10.1073/pnas.1120595109;
RA Arbing M.A., Chan S., Shin A., Phan T., Ahn C.J., Rohlin L., Gunsalus R.P.;
RT "Structure of the surface layer of the methanogenic archaean Methanosarcina
RT acetivorans.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11812-11817(2012).
CC -!- FUNCTION: S-layer protein. The S-layer is a paracrystalline mono-
CC layered assembly of proteins which coat the surface of the cell.
CC {ECO:0000269|PubMed:19228054}.
CC -!- INTERACTION:
CC Q8TSG7; Q8TSG7: MA_0829; NbExp=2; IntAct=EBI-15994209, EBI-15994209;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000269|PubMed:19228054}. Cell membrane {ECO:0000305}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19228054}.
CC -!- SIMILARITY: Belongs to the Methanosarcinales S-layer protein family.
CC {ECO:0000305}.
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DR EMBL; AE010299; AAM04268.1; -; Genomic_DNA.
DR RefSeq; WP_011020873.1; NC_003552.1.
DR PDB; 3U2G; X-ray; 2.30 A; A=318-594.
DR PDB; 3U2H; X-ray; 2.36 A; A=318-594.
DR PDBsum; 3U2G; -.
DR PDBsum; 3U2H; -.
DR AlphaFoldDB; Q8TSG7; -.
DR SMR; Q8TSG7; -.
DR DIP; DIP-60054N; -.
DR STRING; 188937.MA_0829; -.
DR EnsemblBacteria; AAM04268; AAM04268; MA_0829.
DR GeneID; 1472721; -.
DR KEGG; mac:MA_0829; -.
DR HOGENOM; CLU_014690_0_0_2; -.
DR OMA; IDYANAM; -.
DR OrthoDB; 4558at2157; -.
DR PhylomeDB; Q8TSG7; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR026371; PGF_CTERM.
DR InterPro; IPR006457; S_layer-rel_Mac.
DR Pfam; PF07752; S-layer; 2.
DR TIGRFAMs; TIGR04126; PGF_CTERM; 1.
DR TIGRFAMs; TIGR01567; S_layer_rel_Mac; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall; Cell wall biogenesis/degradation;
KW Glycoprotein; Membrane; Reference proteome; S-layer; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:19228054"
FT CHAIN 25..671
FT /note="Major S-layer protein"
FT /id="PRO_0000444298"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 594..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..640
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:3U2G"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:3U2G"
FT TURN 347..350
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:3U2G"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 418..429
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 451..460
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 463..471
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:3U2G"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 481..487
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 494..507
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 512..522
FT /evidence="ECO:0007829|PDB:3U2G"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:3U2G"
FT STRAND 584..591
FT /evidence="ECO:0007829|PDB:3U2G"
SQ SEQUENCE 671 AA; 74394 MW; 4CADDE4851AAED74 CRC64;
MKRFAALSLA ALMLLTVFAS AASAVDVIEI RGPVYNGSDI DDIIDTYGDG TILTMDATDF
AAFYYDIDDN VTTETLSIED VPDTEGNVIG EGGLIYETTI QEVEYEYYNP DAGWDNYSLM
GFFAEKYIPI NPDKADKLSK LILDSDDKYT IRTGEMLDLG EGYAIEAKQV DVDGEKVWLE
FTKDGEFVDD EIISVSTADD EANTWDVELD DIEDEDDVIV LKVHVNQVFQ GAVDSIAQIE
GLWLIDYANA MTIESDDEFG NLDDVSIDGD TLTITNEDTF TLTRDDEEEI GEGLYFATAD
TPSNVLRFYA MKEITDPGTY EIRGQVASGF GDQSWDASSF AGFYYDIDDN VSTETLTVSD
LDGNVIPEGG LVYTTTIADV DFEYYNPDAG WDQYPVMGFF AEEYIPINPD KADKIAKLVL
DSDDKYTIRT GEMLDLGEGY AIEAKQVDVD GEKVWLEFTK DGEFVDDEII SVSTADDEAN
TWDVELDDIE DEDDVVVLKV HVNQVFQGAV DSIAQIEGLW LIDYANAMTI ESDDEFGNLD
DVSIDGDTLK ISNEDTFTLT RDSEEEIGEG MYFMIADTSS SDLRYYPYVE KTIGEEVSGE
EETPEETPTG EVTETEGEEE TPTEVTETPT EGEPAPEETE TTESEGTTPG FGFMFGLVGL
LAVVYLVRRN N
