ID D4TWL2_9ACTO Unreviewed; 1325 AA.
AC D4TWL2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Peptidase, S8/S53 family {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF0970_00322 {ECO:0000313|EMBL:EFF80686.1};
OS Schaalia odontolytica F0309.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=649742 {ECO:0000313|EMBL:EFF80686.1, ECO:0000313|Proteomes:UP000003150};
RN [1] {ECO:0000313|EMBL:EFF80686.1, ECO:0000313|Proteomes:UP000003150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0309 {ECO:0000313|EMBL:EFF80686.1,
RC ECO:0000313|Proteomes:UP000003150};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) 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 -!- 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:EFF80686.1}.
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; ACYT02000012; EFF80686.1; -; Genomic_DNA.
DR RefSeq; WP_003794325.1; NZ_GG753639.1.
DR PATRIC; fig|649742.3.peg.123; -.
DR HOGENOM; CLU_006694_0_0_11; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000003150; 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; 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 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; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1325
FT /note="Peptidase, S8/S53 family"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003064738"
FT DOMAIN 198..659
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 717..833
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT REGION 31..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 616
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1325 AA; 138731 MW; A37BDB48B19EFB27 CRC64;
MTHHSTPALA LAAALALTGV SVPALAASPQ PGGVLPANPT HASSKDTQSG TRVEDALLSI
RQAEAGGATL PDASSAQEAA DDTPTTIIVQ LEDGTAGSST QAMRDDVKAR IASAVAGIVP
GAQVTTVREY TNAFVGFAIE APGSALSAIQ KVEGVKTAFN EGVHKPMDTG AEGSGAPVLK
NASSLAMTRA NEVVLKGDRQ VIEVIDSGLQ TDHDAFAGSM DGVDVRMSQA DVQAFAGKLP
HGGAGTYVNS KIPFAYDYAD NDADVVPHSE KDLSHGTHVT AIAAANADVL QGTAPHAQIV
VAKVASDEDG SMLDSALLAA LDDALVIKPD VINLSLGDDS GMSSDAGSVF AGVYEKLAAA
GITVNAAGGN AFSNAYGNNS GQNKPFATDP DTGTLGEPAS YKSTLAVASV DNQEALSYVS
LGDRTIAYRT ALNGQGEAVR GLRDVPEKTY RIVDAGAGGT DRLEQYAGTD LSGVIVLEDR
GGTDSRDGSA MTEELKARNL TALSPAPAAL MVADTDEAYT PYQAILGSTT SMPTVTITKR
DGEAIREALA AANGADVTVT VTHSGIVLAS NNPTASEFSA WGVAPDLTLK PEIAAPGGDI
MSAYLGNEYQ RLSGTSMASP QVAGISALVR ERLAGDPAFS GMSAEQKNAV VTNLLMGTAH
PLIDVELSDG TYYSPRRVGA GAVDALAATT ATVYPTVVGA ADPSRPKADL GDGTKGWTFQ
VQLTNLSDAA YTYTLGGQAL SEMVEGGLFL EHSQNWVGAG ISLTFSGDGV AEAGDAQQIT
VPAMSNATVT VTVTPESEFA AFASENTPKG TFIDGAVTFT SEDGTPSLTV PYLGFYGSWG
APDVFDGKWS DDETTPVHVF RSALVNAHSS IPLGALNPLS DKQDSNLVTT INTQRLITSR
AKWAGAPDRI APMTGMLRSV PSMSVTYRNS AGELVRSYTI NRVRKSLYDL ETGWTKPGEF
AGEEPFFDGY DQSGNELPDG AYTVTIEAAT DGPSSHTHQM SYEFTLDTQA PVISNLTVSG
EGDARTVSFD VTDASPVAGI DFHEDADGTW YYRKLVEDDG EILADGTHRY HFAVPVSELK
AAWAQQGRTD EAPVTPYLFA WDWGVNPAKQ EVRLQGDPTP APTPAPEPTV DPTPAPEPTP
APEPTPAPSV DPSPVPAPQG GAWISDSVGW WYRYADGSYP RNGAALIDGA TYRFDASGYM
RTGWVSEAGS WFYHDASGAQ ASGWVKDGAS WYYLDPATGR MVTGWLLDGL TWYYLTPGSG
AMATGWVKDG SSWYFMHSSG ALTTGWLRQG SFWYYLSTDS GAMYTGGHWI GWKWHYFAEN
GEWNG
//
