ID Q8TP97_METAC Unreviewed; 1198 AA.
AC Q8TP97;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Cell surface protein {ECO:0000313|EMBL:AAM05420.1};
GN OrderedLocusNames=MA_2017 {ECO:0000313|EMBL:AAM05420.1};
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 {ECO:0000313|EMBL:AAM05420.1, ECO:0000313|Proteomes:UP000002487};
RN [1] {ECO:0000313|EMBL:AAM05420.1, ECO:0000313|Proteomes:UP000002487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC {ECO:0000313|Proteomes:UP000002487};
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., Hedderich R., Ingram-Smith C.,
RA Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA 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).
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DR EMBL; AE010299; AAM05420.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TP97; -.
DR EnsemblBacteria; AAM05420; AAM05420; MA_2017.
DR KEGG; mac:MA_2017; -.
DR HOGENOM; CLU_268697_0_0_2; -.
DR InParanoid; Q8TP97; -.
DR OrthoDB; 103676at2157; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05562; Peptidases_S53_like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR034075; Glr3161-like_dom.
DR InterPro; IPR007742; NosD_dom.
DR InterPro; IPR022441; Para_beta_helix_rpt-2.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR026453; PGF_pre_PGF.
DR NCBIfam; TIGR03804; para_beta_helix; 2.
DR NCBIfam; TIGR04213; PGF_pre_PGF; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF05048; NosD; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00710; PbH1; 3.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002487};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 461..574
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 690..800
FT /note="Periplasmic copper-binding protein NosD beta helix"
FT /evidence="ECO:0000259|Pfam:PF05048"
FT REGION 932..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 128530 MW; AD08BF26433F0A5A CRC64;
MQIAFAAELI QGEYNNGNSS ISADVGGQGY SEETLNPAQM KLSGDLLQLS DERYLSGKES
AEILKARMVE LGQLKQADPV SGRAVLSEEK SEIAAGSGEN AIEASSYPNE KVYVYVYLEP
SANSNILDGY CEVEDRDEKN HIAVAWVPLE SLETLAALSE VRNIQTVLPP FVRQGNTVSE
GDSILNASSL RELYRVNGTG IKIGIISDGV DNLEDVQATG DLPSDVHVLS NNMGGNEGTN
MLEIVYDIAP GAELYFHDCG KSRLEFNRAI DVLVNEGCTV ICDDIGWLAE PFFEDGTVAA
HVKEVIKDHD LLYVSSAGNS GDSHYQGFFY DNGSGWHDFS RGKGEVENLR LEIQPSGKVW
VFLQWNDRWE DSGNNYDLFI KDGNTLETIA SSEVYQDGDN LPLEYIMYTN SGNETLNASI
EVRKTSGEAR ELELYVYYWT GTTLRTTNIV SKDSIFGHPA LPEVITVGAV GIGGSGDYYI
EYFSSIGPVT LYYPSPEIRP KTDISGLDGV NVTGTGGVSE QFYGTSASCP HVAAIAALVW
SSAPEKSAMD IKRLLSTSST DLGEPGYDNV FGYGLVDALK LHEQASAEPS TFTVKTDGKG
DFSSISDAIN SSRPGDTILV YPGKYRENVD VRWALNISSA SGKSADTVLE AKNSGEPVIH
VAANTAKISG FGISGSGETD GSGENGEAGG AGIYLESTAT CTLANNKVSG CSQGVLLEDS
SDNTLTENNI SNNAEGLRLT DSFRNRILEN EFENSINLNE SSSGETGLSN TWNTDTEIRY
LYNGGIYESR FGNFYSDYNG QDADGSGIGD TPYGSDSSPL IARLSAYSRG FEIGSAAPAQ
NTVLIDGNTL EFGIKSTKNC TFSWLLNEAL LQTNEFVPSA TLSVDTGEFA GSITEGNTST
PVPTKYTLTV IATNGSSTLQ HSWTLTTSLI EEETDMPENT SEDSVSRSSK SSGGGGSGES
GGGVAGGSPE PASNVESKEL VQNFVTSGRH IRFDFTRNAT PVTAVEFDAR KNAGKVTVTA
EMLKNQSVLV SGLPEGEVYG HFNIWAGNSG FASPDNIQNP TVSFRVEKDW ISENRIGPAS
VSLYRYSDSN WTELPSRITG EDEAFFYFES ETPAFTTFAV AGQQIGSLQS SSHTPVQNNS
PETGPEGVPE VWITRENTEN STKGGSENGS EDDRSIPAPG FVICIALLLA GALWSKKQ
//
