ID A9G472_SORC5 Unreviewed; 619 AA.
AC A9G472;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Signal peptide peptidase {ECO:0000313|EMBL:CAN98875.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:CAN98875.1};
GN Name=sppA3 {ECO:0000313|EMBL:CAN98875.1};
GN OrderedLocusNames=sce8704 {ECO:0000313|EMBL:CAN98875.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN98875.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN98875.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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DR EMBL; AM746676; CAN98875.1; -; Genomic_DNA.
DR RefSeq; WP_012241314.1; NC_010162.1.
DR AlphaFoldDB; A9G472; -.
DR STRING; 448385.sce8704; -.
DR MEROPS; S49.004; -.
DR KEGG; scl:sce8704; -.
DR eggNOG; COG0616; Bacteria.
DR HOGENOM; CLU_008856_1_0_7; -.
DR BioCyc; SCEL448385:SCE_RS44600-MONOMER; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07018; S49_SppA_67K_type; 1.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR Gene3D; 6.20.330.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047217; S49_SppA_67K_type_N.
DR InterPro; IPR047272; S49_SppA_C.
DR PANTHER; PTHR33209; PROTEASE 4; 1.
DR PANTHER; PTHR33209:SF1; SERINE PROTEASE SPPA, CHLOROPLASTIC; 1.
DR Pfam; PF01343; Peptidase_S49; 2.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAN98875.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 118..267
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 375..531
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
SQ SEQUENCE 619 AA; 64250 MW; 80D206315325EB7E CRC64;
MSKRRARGVR WTGVGALAVA ASMAGCTGRE RAAALPAPAA AGLDEPAVIE IDLSRGLPES
ASASLFGPPS GRTHAQLVQS LRALSESASA KGFLVRLGSA RLAFARAHEI GRILGDVRAA
GRPVVCHADE YNNATMLLAS IACSKLWLSP AGQVDTVGIA AQLVFAKGLL DKLNVDVDFL
QVGKFKGASE PFTREGASPE ARRSLESALG GVREVWLSAI VEGRGKEALR EALEDGPFAP
EEAKARALVD EIGDLESATE DAKKLAGTER SVPRFGGAPR DASFSRSLVD VFRSVSGASS
LGAPHVAVVP AIGGITMSAK GMPIGSSDGI GERELGKTIT RLTEDQSAKA VVLRIDSPGG
SALASDLLWQ KLMRLRQQKP LVVSIGGMAA SGGYYLACAG TKIVAERTSI IGSIGVVGGK
FAVGKALADI GINAETVAAN PDPQRAARAA YMSALTPWDE PTRARVLASM EAVYDLFLKR
ITAGRNLPLE TIAPSAEGRI FGGVEAAGRS LVDELGGLER AIALARELAE LPTDAPVEIE
QDDGGLLELL ATGDEANEGS ARAPDRAALK ERAREAMASV LLPEWLGVAP EVGTFAASMA
PLLAGERALT VLPFAVTLR
//
