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Database: UniProt
Entry: A7BAI8_9ACTO
LinkDB: A7BAI8_9ACTO
Original site: A7BAI8_9ACTO 
ID   A7BAI8_9ACTO            Unreviewed;      1274 AA.
AC   A7BAI8;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Peptidase, S8/S53 family {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACTODO_00652 {ECO:0000313|EMBL:EDN80212.1};
OS   Schaalia odontolytica ATCC 17982.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Schaalia.
OX   NCBI_TaxID=411466 {ECO:0000313|EMBL:EDN80212.1, ECO:0000313|Proteomes:UP000003553};
RN   [1] {ECO:0000313|EMBL:EDN80212.1, ECO:0000313|Proteomes:UP000003553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17982 {ECO:0000313|EMBL:EDN80212.1,
RC   ECO:0000313|Proteomes:UP000003553};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDN80212.1, ECO:0000313|Proteomes:UP000003553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17982 {ECO:0000313|EMBL:EDN80212.1,
RC   ECO:0000313|Proteomes:UP000003553};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Actinomyces odontolyticus (ATCC 17982).";
RL   Submitted (MAY-2007) 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   -!- 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:EDN80212.1}.
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DR   EMBL; AAYI02000004; EDN80212.1; -; Genomic_DNA.
DR   RefSeq; WP_003791214.1; NZ_DS264586.1.
DR   AlphaFoldDB; A7BAI8; -.
DR   eggNOG; COG1404; Bacteria.
DR   eggNOG; COG5263; Bacteria.
DR   HOGENOM; CLU_006694_0_0_11; -.
DR   Proteomes; UP000003553; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 2.10.270.10; Cholin Binding; 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; IPR018337; Cell_wall/Cho-bd_repeat.
DR   InterPro; IPR010435; Fn3_5.
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; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF01473; Choline_bind_1; 1.
DR   Pfam; PF19127; Choline_bind_3; 3.
DR   Pfam; PF06280; fn3_5; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51170; CW; 3.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1274
FT                   /note="Peptidase, S8/S53 family"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002705212"
FT   DOMAIN          195..663
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          467..532
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          699..816
FT                   /note="Fn3-like"
FT                   /evidence="ECO:0000259|Pfam:PF06280"
FT   REPEAT          1193..1212
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          1213..1232
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          1233..1252
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REGION          27..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        271
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        598
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1274 AA;  132263 MW;  E5634CB1CEC2B2D7 CRC64;
     MTTKKPATLL ALAGTAALVV AGPAALASPQ TPADTRPDAG ATASSLPVGD VDTALTSKSG
     ETTQTEQAPT TDEVDPAAVV TIVVQLDDGA DRAASLASIN EAVAGAFPGS STQVEREYDK
     ALQGFALSAP AGSLDAIRAV NGVKAAFLDR DTHVDGVDDQ VAGEGATNSS RIATQDPANL
     SAQLMIHADQ ITQKGDGKVV AVIDTGVDMT HPAFAGALHG TPGLSEDKVE ALTPQLGDGK
     TGSYVSEKFP FAYDYADNDP DASPTGEAGS HGTHVAGITA GNAGEIVGIA PDAQIIVAKV
     ARSSNGGIPD SALLAALDDM VILHPDVVNL SLGQTGGMDN EADSMYATVF KSLQDAGVTV
     NAAAGNEYTA GYGNLSGKNL PFASDPDSSV LCEPASYSSV VSVASVDNSL AHSAFTVGDR
     DIAYQRAGGA DGQKMPDLSD LTGGPFEYVD GGIGSPEDGE ALKAKYPEGL AGKIVLVKRG
     SLTFQDKFNN IAGSKPAGFI VYNNVPGDSL VVMSLATDGV PAAFISQADG EAMLAAADHH
     LSVAPGKVVP PSSKYSMSSF SSWGVTPDLR LKPEVSAPGG NIYSAVPGGT YEFMSGTSMA
     TPQMAGVSAV VLQRVQNDPL FASMSAREKV DVVQNLIMST AAPIVDPLQD TGAPYSPRKQ
     GSGLANVLAA TTSSVYPTVV GAPEQSRPKA DLGDGTKGWH FDVTLHNLSG AEATYELSSQ
     ALSEIVEGGF FTGHSADWRG KGVDIAYSGA AVSGTDEGAI ITVPANGEAT VGVDVKPGTD
     FDASIAQNMP NGTFLDGFVR FTSKTASQPD LTVPYLGFYG NWGKAPIFDA LASEDGAHTL
     ASWVYNGTTG QQLGYNPLVK DADRIGLPTS SKNVISRSDA SGAPTVLQPR TGTLRSVHTL
     NAAYTNAAGE TVASFTRFMN WKSALDSSTG KMTWVEQGHD PMSLDARADA YKNLPDGTYK
     LTLSAHNDGP SQADQSISYE FRLDTAAPVV SNLEYKGEGA DTVLSFDITD ASLLAAIDLH
     DPADGLWFYR HIFTDNEATT AADGTRAYHV EIPFKDIAQA WTDQGGSGEV IAHPYLLAWD
     YGLNHSEALT LNLPSDNTGT ADACASTEGG HWTKDAAGWF YTCADGTSYL KGGWYTINGS
     DYLFGPSGYM ATGFLKRADG QWVYANESGA LVGGWVRDGG SWYYLDPTTK VMATGWVADG
     GSWYYLTSSG AMAIGWVQVD GSWYYLSGSG TMATGWIKVG GLWYYLGPDG AMLTGTQVIN
     GRTYVFDGSG VWVG
//
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