ID F1Z0H9_9STRE Unreviewed; 1618 AA.
AC F1Z0H9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=C5a peptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SPB_1901 {ECO:0000313|EMBL:EGE53290.1};
OS Streptococcus parauberis NCFD 2020.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=873447 {ECO:0000313|EMBL:EGE53290.1, ECO:0000313|Proteomes:UP000003732};
RN [1] {ECO:0000313|EMBL:EGE53290.1, ECO:0000313|Proteomes:UP000003732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCFD 2020 {ECO:0000313|EMBL:EGE53290.1,
RC ECO:0000313|Proteomes:UP000003732};
RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA Town C.D.;
RL Submitted (FEB-2011) 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:EGE53290.1}.
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DR EMBL; AEUT02000001; EGE53290.1; -; Genomic_DNA.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_001768_5_0_9; -.
DR Proteomes; UP000003732; 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 Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-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; PF06280; fn3_5; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1618
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003272528"
FT DOMAIN 211..695
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 718..832
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT REGION 46..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1158
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 277
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 623
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1618 AA; 182056 MW; C3F9C7B164075E38 CRC64;
MKEKKICKIA ILSLVCPLTL LLTSQAAAAE SQNENTSNYL SKVKADESRS LEVENASNSS
SPMSIYEEKA TNQSSAFVEQ TNSENESTNK SEPLPTNHVN LEQPIRSENA DEASSHGIKE
YEIEFDQKTK YVNDELIAML AKKEEKGKQS LNDSKVNIQV PEQFSYYLNK LVGVKNIKEI
ANTNLEKSEK EALTKLIDSY IKSTNDRKFD GRGIVIASVD SGADVNSQDM TIDQDPNVKK
HLKLAANKDL GFTEKIPFGF NYLTGTYDIK DRSNRPHGMH IAGILAGNSK IPGGFKGIAP
NAQILSYRVF STEPKDEDNP SYVGPDSKFH AIDDAIRRKA DIISLSIGER ASGLSDDDFY
AAVKKATDEG IIVVAAMGNY AGSASTNSYD TYVDNEYRLK DTSTAVGVAA TESAIGVGSI
NNMVVPLPRV LIDGKEYPFT EVGAHSIKRL PKNKEDFGII YLGKGTPEDI AKYNPNNDSY
KDKVVLIQRG DESLKTKVER FLKNSKGVIL VNEIVSSTRG NYHRAPVMGY DDLDLKQNWV
ISLSHDDGKE LIDKVQKLGN KKVNLQFKTE LKPYIIADQN GVSGFSSWGP NFGLEMKPDL
LGQGEYIYST RNDDDYFISS GTSMASPHVA ASAALLLPKV KEWINQNPEL KSRFQLTNSD
IMKILLMNTA TPLINHQASD LGKEIEHSPR QQGAGFINVN KAFNSEVLIR SKRSGGASLG
EIGKDHSFTL TLHNMSNQSQ TFDIEMGDIF TTSVKEVTRD DEYGPVKIKA VIPNILSDVK
LSGPKQLTLA AKGSMEITFN LQSSELINDF IEGYLYFKSH DGKHPHLSVP FMGFMGDWNS
EAVLDKPAWD KDANTHLVEL VKEKYLEHDK NDYEPLIKHE SDEAVNPKDY AMTTNLNRKV
GPRLIFLRDA SDYDVAIVKG EQKDQLVRVL KVGHYPFKYM ESSYRESADL KAKLENIDSD
ILWDGKIHDE NSFGELKKAD PGQYYFRIRA KAGKSDEFET IYLPILIDNE KPDFDLKYKK
QTLQISATDN HKVESVKVSL EKGYRYEALN VSKDQNDSYV VEIPKKEGGQ VTLRIVATDI
AGNACEKTVV LDQNGKLTVK EETLSNYNYQ PKKSDDNYDE AENDLHSLAR HELEDRADSD
DDDDDWSDDE EDDEDSDIDA HNIVLTHGKE ITLHTLASLQ ENHITYDDNS KIATLDYAIY
LKKGYQARVR NINTQYNSLQ NNLSDPYKAM YDTTLKYEND SYNKESQEYN TKKVPDKLKL
ANGNNLVYVD ILDEKGSTVF HKNYFIFVDL ETPTLELLNK EVFKDDEDLT PVLDTSNDSD
DLDDFEDANE SDTSQLGYYK GIIKTNTNQL TMKFSVKDNL DFWKLYVNND MIDSFSLDGY
YQKNQKFVSY TMPVKDKQKI CVRLEDRYGN SVEDHYVVVI DPTYQDKKDV IQASTLVTAK
SYWNQTSTLP VKVKQGILER GKEYSINDLI EVGEGTSYSI KEPLSTQQEG IKKLSIELFK
GNTRQFQILT FTITDPQSDN IQKKEIKDLP LTEDESQKQV DDLNSQEVIQ VQDGLNIINP
IPLKIKETQK HQQKVQGNRG HTLPETGSRD DCSKLGALFS VVMSLAIFLK NPIKGKKF
//
