ID G2LFW0_CHLTF Unreviewed; 606 AA.
AC G2LFW0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Signal peptide peptidase A, Serine peptidase, MEROPS family S49 {ECO:0000313|EMBL:AEP11754.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:AEP11754.1};
GN OrderedLocusNames=Cabther_A0998 {ECO:0000313|EMBL:AEP11754.1};
OS Chloracidobacterium thermophilum (strain B).
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP11754.1, ECO:0000313|Proteomes:UP000006791};
RN [1] {ECO:0000313|EMBL:AEP11754.1, ECO:0000313|Proteomes:UP000006791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:AEP11754.1,
RC ECO:0000313|Proteomes:UP000006791};
RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x;
RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M.,
RA Bryant D.A.;
RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a
RT chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria.";
RL Environ. Microbiol. 14:177-190(2012).
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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DR EMBL; CP002514; AEP11754.1; -; Genomic_DNA.
DR RefSeq; WP_014099492.1; NC_016024.1.
DR AlphaFoldDB; G2LFW0; -.
DR STRING; 981222.Cabther_A0998; -.
DR KEGG; ctm:Cabther_A0998; -.
DR HOGENOM; CLU_008856_1_1_0; -.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000006791; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
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; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR004634; Pept_S49_pIV.
DR InterPro; IPR004635; Pept_S49_SppA.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047217; S49_SppA_67K_type_N.
DR InterPro; IPR047272; S49_SppA_C.
DR NCBIfam; TIGR00705; SppA_67K; 1.
DR NCBIfam; TIGR00706; SppA_dom; 1.
DR PANTHER; PTHR33209; PROTEASE 4; 1.
DR PANTHER; PTHR33209:SF1; SERINE PROTEASE SPPA, CHLOROPLASTIC; 1.
DR Pfam; PF01343; Peptidase_S49; 2.
DR PIRSF; PIRSF001217; Protease_4_SppA; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEP11754.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006791};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..289
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 385..536
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 203
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 402
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 606 AA; 66192 MW; 5670F678C77AF4C9 CRC64;
MRDFLKYVFA SLTGTLIFFG LVLGGILLLL ASVASLSSGR SPEPAVQDKT ILVFDLSATI
SDIAPSDDGR EVDVQRLLRG SGGKILPLST ILDCLDKAAA DKRVVGLYLH GNLSTEGYGS
GFAALREIRE ALLRFKASKK PIYAYNQVYS ERDYYLASVA DKIFLNPFGA IEMNGLASEM
MFLGEAFKKY GVGIQVTRVG KYKSAVEPLL FDKMSPENRE QTQKLLDDVW GEFVSGVATA
RQLTPDDLQR LANEKAILVG PEAVAAKLAD ETAYLDQVLG TLRKLSEVKD DKAPFRQVTL
PAYARVSRRS LGLERTSRNI IAVVYAEGEI VDGAGSDGQI GGDRLAKELR RLRQDDQIKA
VVLRVNSPGG SALASEVIRR ELAETRAAGK PVVVSMGTVA ASGGYWISTA SDKIFAAPNT
ITGSIGVFGI LPNIQKLAGD YGVKWDTAKT NRYADLGTIT RPKTEDELKL IQANVDRIYD
EFLTRVAEAR KLPKETVQEI AQGRIWSGAE AKRLGLVDEF GGLEAAIQAA AELAKLGNDW
KIAEYPKRRN LAEQLAKLLT DEEPERLVQG PVQRELEQLW AETAALAAFN DPLGVYARLP
FLLRFN
//
