ID A0A410E0I4_9CLOT Unreviewed; 1718 AA.
AC A0A410E0I4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 02-APR-2025, entry version 30.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:QAA34825.1};
GN ORFNames=C1I91_26085 {ECO:0000313|EMBL:QAA34825.1};
OS Clostridium manihotivorum.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2320868 {ECO:0000313|EMBL:QAA34825.1, ECO:0000313|Proteomes:UP000286268};
RN [1] {ECO:0000313|EMBL:QAA34825.1, ECO:0000313|Proteomes:UP000286268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT4 {ECO:0000313|EMBL:QAA34825.1,
RC ECO:0000313|Proteomes:UP000286268};
RA Tachaapaikoon C., Sutheeworapong S., Jenjaroenpun P., Wongsurawat T.,
RA Nookeaw I., Cheawchanlertfa P., Kosugi A., Cheevadhanarak S.,
RA Ratanakhanokchai K.;
RT "Genome Sequencing and Assembly of Anaerobacter polyendosporus strain
RT CT4.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP025746; QAA34825.1; -; Genomic_DNA.
DR RefSeq; WP_128215536.1; NZ_CP025746.1.
DR KEGG; cmah:C1I91_26085; -.
DR OrthoDB; 9762689at2; -.
DR Proteomes; UP000286268; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02133; PA_C5a_like; 1.
DR CDD; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR InterPro; IPR044016; Big_13.
DR InterPro; IPR010435; C5a/SBT2-like_Fn3.
DR InterPro; IPR034216; C5a_Peptidase.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR050131; Peptidase_S8_subtilisin-like.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR43806:SF11; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF19077; Big_13; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF09136; Glucodextran_B; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000286268};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1718
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039200849"
FT TRANSMEM 1694..1712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1685..1718
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 1647..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1681
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 250
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 578
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1718 AA; 182221 MW; C861BCA84AEC798E CRC64;
MKNRVVLSKT ISALVALALV VPNGFTRQVK ALDKKITGAN DIKAIATEKY KNSLAKKADK
LKGKQPNDSV RVVVELDGKP ALDKAREKGL KSAVKSDIQS VKDSQKTVQD NVKEITGNKI
RNTFGTVVNG FSIDAKVKDI DNIKKLKGVK DVKVVNVYYP DMNTAKELTE ATKVWKDLGL
KGEGMVVSII DTGIDYTHKD MKLTDTSKEK LTEANIKKGG PGKFYTDKVP YGYNFADKND
EVRDTTSSMH GMHVAGIVGA NGSDADIAAN NGIKGVAPEA QLLAMKVFSN NPQIQGAYSD
DIVAAIEESV NQGADIINMS LGSTASFQED DDPEQVAIKK AVDAGTVVVV SAGNSQYSTA
PYKQSNMTDT GLVGSPGLAK DALQVASYEN TSVTLSAITL EDGKETKAGY TTSDVLPSKV
LDPTKDFEIV DCGLGQASDF TGKDVKGKVA LIKRGSINFV DKKKNAQGQG AVAAIIYNSE
AGGDAYINMA TDPSITIPGV FVTNTDGKKL ADLAKNGGKV KFGTERVITP NVNAGDFSDF
TSWGPTPNLD FKPQISAPGG NIFSTVNNNQ YEVMSGTSMA SPHVAGSEAL IVEALKKANP
NLKGRDLVDL AKNTTVNTAT IEMDKYHTDT PYSPRRQGAG MIQTEKAINN KVTVTNDGNS
YVALKQIGNE ASFDLTLKNY GDKDATYDLE NYGGVLTEQD QEFISTMSYD VKVDGAKVTF
DKSSVTVPAN GTATVKATLT VPKTVSENRF VEGFVKFNAS NVPALVIPFM GYYGDWGKEQ
IIDKMNYDGD PIFAVSSSAV TSLGDKYMPL GVTGKDSRGD DIVDKDYIAI SPNDDSLFDN
FVPDLYFLRN AKNVDVELSD ETGKVLGLVA NDKDIRRKVY NDTDGSGKVA SVYNSLAWDG
KLYDPTVGVK RAVADGKYYL NIKATVDFAG AKPQDYKIPV KVDTTAPEIK LVSAVPNAAA
TNGVASYHIT LEAKDNLAMS KEDPVVLLNG QLDQDIKNLQ VNGGTYSFDA NLKADSINDL
SVALPDSVYN IGSNDFKINA GSSAPVLFYD DKFTKGFDSP VDTYTVEGKV NTQLKTFKIA
NQDVKVKDDG TFAVELKLNQ GVNVIPIYAE DLSGNKLINY STKINCDSIA PVINLASPAV
NGDGLIVTNQ DSITLNGTVE DNGWGYKFEI NGEVALNVNV DGATGPEANK KDFSKTIAVK
DGDVISLKAT DTFGNITENK ISVRVDKVAP ALTISGVTDG GLYNKSVTPV VTADKKATLT
LTLDDKAYSG AAVDAEGKHV LKAKAVDEAG NVTEASVTFE IDKTAPTLSL TGVEDGKLYN
ADITPAVQTE AGATVKASLD GNAYDFKAVT AEGKHVLEVT STDKAGNQST VKVSFEIDKT
APVFNVKNIE NGATYLDNVT PSITVDDKTS AVSLLLDGKA YDGAAAIASE GDHVITGTAT
DKAGNKSAIE IKFTVKQSVK TDKNSDGSVN VSVRKPLDKD GSNVVTSDAT NSASFAFENA
DAMKGGKGSF TLNVGANSIN LPFAAFDPNL ISNGSSVVIN AKVDENSPLT KGLKAVNKVF
TFEALIDGNG KQTPVHSFSN EALATITLTF SDDELKGLDR SKLAVFYYNE TTKAYEEMAT
KVDGNKVTFN TPHFSSYIVA EKQVASNTTG TSTTTTTNSG SASGSSANTT ASTGSTATTS
TPAAMPKTGS VIDSNILVIL GLMALAGGAV IIRRKRFN
//
