ID A0A1H0VWD2_9CLOT Unreviewed; 1555 AA.
AC A0A1H0VWD2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Lactocepin {ECO:0000313|EMBL:SDP82882.1};
GN ORFNames=SAMN04488529_12111 {ECO:0000313|EMBL:SDP82882.1};
OS Clostridium gasigenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=94869 {ECO:0000313|EMBL:SDP82882.1, ECO:0000313|Proteomes:UP000198597};
RN [1] {ECO:0000313|EMBL:SDP82882.1, ECO:0000313|Proteomes:UP000198597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12272 {ECO:0000313|EMBL:SDP82882.1,
RC ECO:0000313|Proteomes:UP000198597};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNJM01000021; SDP82882.1; -; Genomic_DNA.
DR STRING; 94869.SAMN04488529_12111; -.
DR OrthoDB; 9762689at2; -.
DR Proteomes; UP000198597; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR InterPro; IPR034216; C5a_Peptidase.
DR InterPro; IPR010435; Fn3_5.
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; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF05922; Inhibitor_I9; 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; 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:UP000198597};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1555
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011456096"
FT TRANSMEM 1530..1547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..170
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 192..647
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 437..517
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 672..787
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT DOMAIN 1513..1550
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|Pfam:PF00746"
FT REGION 1467..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 585
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1555 AA; 169808 MW; B289B866CDB922DA CRC64;
MKKVKKKVIA IAVTTMFVVN CSSLVVSAKE TGEKENFLRT ELLQNLKSEI NEGDKFSNIK
QLKEEDIENL SLKESGNPEE RVRVIVELKE KPATLKLEDG EQPTKEQIQE VKDDQKPIQE
DVEEKTGEEV RHTYGNLING FSMEVKRKEI DEIKTVDGVQ NVKEVNKYYL DMSTAKELTQ
SLDVWKDYGY KGEGLVVSVI DSGVDYTHKD MRLTDPSKAK LNKDNLRDGK GKYYNDKVPY
GYNFADENDE VIDKGSMHGM HVAGIIAANA TEADVKSDTG IQGVAPEAQV LAMKVFTNNP
EIETAYSDDI IAAIEESVEQ KADVINMSLG APAGFRDSEN PEQAAIKNAT DDGVICVVSA
GNSAASTSPT IYEDFSDIAT VGTPGLASDA LQVASSENTT IPLHAFNINL NGENNLAGYT
LCKVNPRDTF TDGEELELVE CGKGTENDFK GKDLKEKIVL VSRGEISFVD KQINAQKAGA
KGVIIYNNAV GGYISMQSDE SIKIPSLFIS QEDGLKLSGG IAKGVKISFG NYKVTKANPE
TEMMSNFTSW GPAPNLEFAP HITGPGGNIF STLNDNRYGN MSGTSMASPH VAGATALIIQ
GLKAKGINLK GREFVEFVKK SIINTAKTIE ETNKLGEKVP FSPRRQGSGI IQTKEVINNR
VVAFGKDGQA TVSLKEIDEV TEFEIKLKNY SDKEESYKVE SLGEVLTAFT PSMANEKSLN
AMPFDTTLNG ASINIDKDKV TVPANGETTI KVTLNVKEDS VKDNFVEGFI KFIAENQDTP
SLVVPYMGFY GEWDNQKIID APVWEKDDIR ILPSYTVAEV LGKLNYLGFN GRDANDDIVI
DPNKIAISPN SDELGDKIIP TLYMLRNAKE IQVDVLDENK NVIAENISKE QDVTKKIVES
KTGKEASAYK SLAWDGTAYN KATGKNEKVK DGQYYLNYKS KVDGDGAKYQ DYIVPVKVDT
EGIETKLISA DKSDAPDYKL QVSFNGEYEK GLVNNVGLSV NGEKVEGFTV KGDTLTADLK
LNNDSANEIK VATLDNAYNL KDTNFKVSVG KVETQVKFTD FEEGATVTDN KLVVNGTYSG
DVDTILVRGE APDKMENGKF SKTIALTDGL NTINLFAKDK EGKVIRNDAY RIFCDTQAPV
LNITEPVSNH EGLVVTAKDV VTLKGTVSDN LMGYNLFVNG ENKLNISSDG KYAEQYTKRE
FSYDIPVADG DIITLKAVDS VGHETLKQLK VKVDKTIPEI NVYGVENGAI YNKNIKPNIT
VKTELAKLEM TLNGAKYNGE EIVEEGNYEL VAKAVNANGL TRDIKLNFTI DKTAPTINIG
NIEDGKKYNK EVTPKFEIEE GATTSMKLNG KDYNGEMIVE EGNYELVVKT ADKAGNITEK
TMKFDIDKTA PAVSLDDAID GMTYNKEVKP VVNSDKDANV SVTVNDKPYD GQAIKENGEY
VVKVVAKDEA GNVTEVTRKF TIKLPEADTK NPTKTPASTS KQVENLGGEV SDDKKNAETE
KVLNANNTSN SKEAASKGNI PKTGGVNSNA LIAIGVVVLA AGIVLIVKRK SKSIK
//
