ID D7BP86_ARCHD Unreviewed; 1782 AA.
AC D7BP86;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ADH92735.1};
GN OrderedLocusNames=Arch_1015 {ECO:0000313|EMBL:ADH92735.1};
OS Arcanobacterium haemolyticum (strain ATCC 9345 / DSM 20595 / CCUG 17215 /
OS LMG 16163 / NBRC 15585 / NCTC 8452 / 11018).
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Arcanobacterium.
OX NCBI_TaxID=644284 {ECO:0000313|EMBL:ADH92735.1, ECO:0000313|Proteomes:UP000000376};
RN [1] {ECO:0000313|EMBL:ADH92735.1, ECO:0000313|Proteomes:UP000000376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9345 / DSM 20595 / CCUG 17215 / LMG 16163 / NBRC 15585 /
RC NCTC 8452 / 11018 {ECO:0000313|Proteomes:UP000000376};
RX PubMed=21304742; DOI=10.4056/sigs.1123072;
RA Yasawong M., Teshima H., Lapidus A., Nolan M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y., Jeffries C., Rohde M., Sikorski J., Pukall R., Goker M.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Arcanobacterium haemolyticum type strain
RT (11018).";
RL Stand. Genomic Sci. 3:126-135(2010).
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; CP002045; ADH92735.1; -; Genomic_DNA.
DR RefSeq; WP_013170231.1; NC_014218.1.
DR STRING; 644284.Arch_1015; -.
DR KEGG; ahe:Arch_1015; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_001768_2_0_11; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000000376; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
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; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
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; 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 InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF06280; fn3_5; 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; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000000376};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1782
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003093521"
FT TRANSMEM 1752..1778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..625
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 417..471
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 647..750
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT REGION 1194..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1534..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1703..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1232
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1709..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 227
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 565
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1782 AA; 191777 MW; C39894139A8A9D07 CRC64;
MRRLFSSVAF ASVVSISLGL APCATASPFV EKPHSAGSEL SFHDMEEILG RSATAESKRA
RVLVMLKDQE FDPSESSEEK HIETQEELLS RWQKKYGLKV RRQLGYLVNG FSADMPVKKM
AALQNEPRVS SVKFERTYAR AEHNARQMEG VPQAYERHGL DGTGVVVSII DSGIDPTHKD
LKFTDEDCKK AKLKPDTKHS IFTCKVPTGY NFADENFEIT DKNKSEHGQH VSGIVAANGS
AHGKADVVEN QSFDGVAPKA QLLAMKVFSN KPDSRASDSD LIAAIEKSVK LKADIINMSL
GSANGNRNAS DGVFRAIKKA REAGVMVVVA AGNEGLNFSE NGDTNDTRGQ LDDGTLGSPA
ADTGAFAVAS LDNAVQVLPL AKWKKKDGKE ENLIHKTSTG KPDNTEHTIV DFGYGGAGEF
TPEKKAQVKG NIALIQRGKE KFSDMFKRAI DEAGAIGVLV YNDEKRGEEF IGMGGVEKYT
QFSASTYHSV GVKIAEAIKQ GEVKVTFTDK RQLVDYAGKK HLRPSSFTSW GPTPTLDFAP
HIAGIGGEVF STLNKDRYAS DSGTSMAAPN VSGLSALLWQ HFTKQNPKMS RVDIVKRIRT
ALMNTAQIPT NEQNVPYAPR QVGAGLARVD NAAEANVTAT VDGEPFVSLG ELSGPKSFTV
TLHNHGSMAA VYSVPAQRVV NETNGVNEKT TTFVATKESL TADRDSVVIQ PGAEEKITFT
VSPAVGTDHY IEGWAELKGT QVPDLAIPYL GFVGNWNKEA IIAPAGEQWG DPVKVKASTV
LATLREDSAV PLTEVQDLAE NKDNKRDLSL WISPNGDQMQ DVVFPQMLIR RNAADVEYSV
TSEDGKFKQT TGKQQDLRRP QLKHAVEPGA TREDILFTAG AYGFDGKIYD KKNVKYTVVP
DGKYVFHIKS RVSEKHPWQE VKLPFGVDTS VPKITIGEYD GEYVNFDVVD EGSGIQVKPI
AETDRAVNIV SERINESDTH FRVKVGKDAK YVAITAGDMA ANVAREHKIL HDDKLAIAFE
TAMTKKLIGD VTPFVVKYGE PAGPKAVISG YVAPEVDSLT VNGKNVEIDK HHFETLAPLT
VGENKIEVKA FDKTGKVLKS IVLTPYYDNV APTLKITERK IDGNKATISG TIADNSDLAE
LSVIANGQNA TLSDDVTKNS KTFTVTVDFD EETQEITVVG SDGGNRTTKT VSVTGDFTPD
PAGPGGPGVP PPPPPLPGGP GVPPPPPLPP GGFTSFSANL PKIDNATCGQ NIPVCAVPNT
TPDYDRATKT FTLRGTVNAG TVAKLQLVPS GDDRDGVMAE GKPFVATIQK DGKFALPVHA
ETGQNHYRLE LFVAGEKEPV RTKAQSFKLL IDVNVPTVTF SEPNVIAGSI FTNQDAVTFT
GKVSDDGWGY KFLINKDTVE ERENEAGHGP ESNEREFTYP VKVEDGDKVL VTVIDRFGNQ
ILGVYPVVVD KDAPVVGFTQ EKQPVVDGRR LESDATIVTK AEDKNLRGFT LSVVDHKGKQ
IFTDTQYSDV EMTEKKPEEL MADVREIRKE ALARSAEKKR LEEKETETGD KAAEQPKDEV
VVSGSKATVT ARELAIPFAV DKLPAGNYAM TATATDLAGN QTVSSVSIVV DRIPTIKGPE
SVDVTVAKSQ LAKFATIGEQ VFSHYTIDDD GVADLLGTGG VEGETELQFA SGTEFKEGAN
TVTIRAVQPN GLESSRVIAV KVTIDDSKDT QPDSSNNGGE EDRTPGTQGG NSDRPGRTIP
VPPTQVASAG KALAATGTVA GALGLVAMAF IAAGAVIARR RA
//
