ID D9PQA0_FINMA Unreviewed; 2037 AA.
AC D9PQA0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Serine protease {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=HMPREF9261_1417 {ECO:0000313|EMBL:EFK94271.1};
OS Finegoldia magna ACS-171-V-Col3.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=768713 {ECO:0000313|EMBL:EFK94271.1, ECO:0000313|Proteomes:UP000003650};
RN [1] {ECO:0000313|Proteomes:UP000003650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-171-V-Col3 {ECO:0000313|Proteomes:UP000003650};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Nelson K.E.;
RT "Genome Sequence of Lactobacillus delbrueckii subsp. bulgaricus PB2003/044-
RT T3-4.";
RL Submitted (JUL-2010) 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:EFK94271.1}.
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DR EMBL; AECM01000011; EFK94271.1; -; Genomic_DNA.
DR RefSeq; WP_004166994.1; NZ_AECM01000011.1.
DR Proteomes; UP000003650; 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; 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; IPR046450; PA_dom_sf.
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; SSF52025; PA domain; 1.
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..2037
FT /note="Serine protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003126182"
FT DOMAIN 224..717
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 796..933
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT REGION 1345..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 300
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 691
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 2037
FT /evidence="ECO:0000313|EMBL:EFK94271.1"
SQ SEQUENCE 2037 AA; 229010 MW; 29D86848A9FE0818 CRC64;
MKKKDIIKAT LVAALSVSSV SFMCSDTVFA KIEDTENIID NEKSIEYKQD GNKLTNETLK
VNKENSNNTN DEKLSVITKE DIKEDSAIDN KNTSDNKYSN KEVSKGNELY KADEIQNISK
KEEDRVVYIA EFRNKEDGQK AIKELSNFKN TKVLYTYNTI FNGCAIETNR DNLDKIKLIE
GISSVEKSQK IQPMMNNARK EVGVDESIDY LKAINAQFGK NFDGRGMVIA NIDTGTDYRH
KAMRIDEDAK SSMKYKKDDL QGTDKYFWLS DKIPHAFNYY NGGKITVEKY DDGSDYHDPH
GMHIAGILAG NDTDEDIANY NGIDGIAPNA QIFSYKMYSD SGDGFAGDET MFHAIEDAIK
HKVDVVSVSS GFTGTGLVGE KYWQAVRALR KAGIPMVVAT GNYATAASSS SWDLAANNQL
KMIDTGNVTR TAAHEDAIAV ASAKNQIVEF DKVNIGGESF KYRNIGTFFD KDKIIRNEDG
SKLSDKVKFV YIGKGQDEDL VGLNLKGKIA VMDRIYTKDL KYAFKKAADK GARAIMVVNT
VNYYNRDNWT ELPAMGYEED EGTTCQVFSV SGDDGLKIWN MINPTNKTEV KRNKKEDFKD
KLDQYYPIDM ESFNKNRPKL GDEKELAFNF APDTDKELYK EEVIVPAAST SWGPRVDLLL
KPDVSAPGKN IKSTLNVIDG KSTYGYMSGT SMATPVVAAS TVLIRPKLKE MLAKPVLKNL
TGDDKIDLTT LTKIALQNTA RPMMDPTGWK EKSLYYASPR QQGAGLINVA NALRNDVIAS
FKNLDSEGLV NSYGSISLKE IKGDKKYFTI KLINTSDRPL TFKASSSAIT TDSLTNRLKL
DETYKDEKSQ DGKQIVPEIH PEVINGAKIT FEYDTFTIKP NSSFDLNAVI DVGDAKDKNK
FVESFIRFES KEEVEAMCGK GNKTVFQPSL SMPLMGFAGN WNKEPILDKW AWEEGSKSKT
MEGYDDDGKP KIPGTLNKGI GGEHDIDKFN PAAVIQNRKD GNTKSLDQDP DLFALNNNQG
LTDASNSGSK VARVYPLDSK GQNQEVQIER GLTPSPLVLR SAKEGQISIV NTDKEGEGQK
DLKVITKEHF IRGILNSKRN DAKGIKSSKL KVMGDLKWDG LIYNPRGREE GANDDNNNQD
LETKLRGQFE PIAEGQYFYK FKYRLTKDYP WQVSYIPVKI DNTAPTIVDV DFSNPDKIKL
IAKDTYHKVK DKYKNETLFV RDQKNHPDKF EEVANEVWYA GAAIVDENGD VERNLDVKYA
GEGEGRHRKL DEKGNTIYEI KGAGDLRGKI IEVIALDGAS NFTKIHRIKF DNKADAKGMI
SYYLVDPETD ASSYKKLGEI SEEKLKNAQS PEASNKAEEK KDTVEENPIE GPSNLELNKE
ISTVRGFEDK DLKKLVKKKY KQEDDYVNGG KRTVELDYQY DENGNIKAYE DGSALEYETE
KLYDVKSKLG GVLSPSKDGH FEILGRVSNV SKDAKAYYGN DFKLIEIKAS KYDPQTKTLT
FDLFANTNDV VDGLSFTGDM NIIVKDKDQT KAKTIIRMPE KKDEAEEASP YASSYGNIIE
LGEGELTKQK PQDPSKMDTN KMFFDQEKGQ YILNDNMIVR KGYALRVTTF NPGKTDMLDG
NGVYSKADIE KIQKTAPNIK VLSQKTIYCD SRNVQDGRSA QSVLMSALDG FNIVRYQVFK
FKTNDKGEAI DKDGKLVDDP SKLVLLGKDG KEYIGDDKSN VEAIKEDGAM LFIDTKPVNL
SMDKNYFNPS KSNKIYVRNP EFYLKGKISD KGGFNWEMRV NESVVDNYLI YGDLHIDNTR
DFNIKLDVKD GDIMDWGMKD YKANGFPDEV KDMDGNVFLK TGYSSMNAKA VGVHYQFLYD
NVKPTVEMSE DGKISIEYAK NKFIKFNIFD KRNNNKDGEI QEQHIYVNGK EYKSLDDIKD
IKDNELKIKF VVKDFARNTT VREFNLNKNT GTVAPIESEK VKLTIDNKEN ELVKGEDFVL
PAYNGEVAEG YQFDGWEISG VKDKKESGYV LFVTEETKIN STFKKIKVKE QEENKPT
//
