ID C0CYB2_9FIRM Unreviewed; 656 AA.
AC C0CYB2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=TIGR02594 family protein {ECO:0000313|EMBL:EEG55967.1};
GN ORFNames=CLOSTASPAR_01988 {ECO:0000313|EMBL:EEG55967.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG55967.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG55967.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG55967.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG55967.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG55967.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C40 family.
CC {ECO:0000256|ARBA:ARBA00007074}.
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:EEG55967.1}.
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DR EMBL; ACCJ01000107; EEG55967.1; -; Genomic_DNA.
DR RefSeq; WP_007709578.1; NZ_GG657591.1.
DR AlphaFoldDB; C0CYB2; -.
DR MEROPS; C40.007; -.
DR HOGENOM; CLU_012396_2_0_9; -.
DR Proteomes; UP000004756; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR47053; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR PANTHER; PTHR47053:SF1; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR Pfam; PF00877; NLPC_P60; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 527..654
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 72749 MW; C455C526EF651F95 CRC64;
MSKELKAPDK VTQKMTRDGA VAENLTTGET TSISERPPEE NYSAPVAGAA EKATQRIGTE
VSRHFEKGAE KKTLDAAQLK THTSRLQFSE AERATPDLQK AIKKSDTAAD RLDKARAAIP
KQTKITKERV FDEAKGKAKT RLAFEKTDKP PNGKLRHNPL SRPAQELDAA VHGKIYEVEK
ENVGVESGHR IELVGEKAGG MTTRAVKRGI RSHKLKPYRA AAAAEKKAAK ANADFLYQKA
LHDNPALAHS NPISRFWQKQ RIKKQYAKAL KTGGKVKKTA EATAKAAKKT AQETKRATFF
VVRHWKGCLI VGGIAFIVLL FFGGLSSCSL FGGNSGSGLI ASSYLSEDAD ITGAESAYVA
MEAELQDMLD NIESEYPGYD EYRVTADEIE HDPYVLISIL SAWHEGVFTL DEAQSTLEML
FDKQYILTVT EEVEVRYRTE TRTDSEGNEY DVEVAYNYYI LNVDLENFNL SHVPVYIMGE
EQLSMYAMYM SSLGNRPDLF PQSGYISKYY ENPPADYEVP AALLNSDEKF ARLIEEAEKY
VGFPYVWGGS SPETSFDCSG FVSYVLTNSG LYNTGRLGAQ GLYNISTRVS NPQPGDLVFF
TGTYDTPGVS HVGIYVGEDG DGSPVMLHCG DPIQYAKLDT SYWQSHFYAY GRLHYN
//
