ID A0A1Y1RK71_9BACT Unreviewed; 575 AA.
AC A0A1Y1RK71;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Signal peptide peptidase SppA {ECO:0000313|EMBL:OQY29443.1};
GN ORFNames=B6244_03455 {ECO:0000313|EMBL:OQY29443.1};
OS Candidatus Cloacimonetes bacterium 4572_55.
OC Bacteria; Candidatus Cloacimonadota.
OX NCBI_TaxID=1971726 {ECO:0000313|EMBL:OQY29443.1, ECO:0000313|Proteomes:UP000192623};
RN [1] {ECO:0000313|Proteomes:UP000192623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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:OQY29443.1}.
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DR EMBL; NBMB01000009; OQY29443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1RK71; -.
DR STRING; 1971726.B6244_03455; -.
DR Proteomes; UP000192623; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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; 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 SUPFAM; SSF52096; ClpP/crotonase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 115..261
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 356..505
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 183
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 371
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 575 AA; 64030 MW; 3AF84BF92F044CB9 CRC64;
MKKWLLLIGF IGILVIISII IAGLAVRGMI GSDPVKISSD SILNLDLGGY YPEVSEDDVS
DAILSKEAIT HRRLELMFDT AKTDGRIKEL YIDMSDFGGM GWARAKEIRN WILNFKTSGK
PVTVYMDFVG DRTYYVATAA DKIVMPPEGG LLVNGIALQM FFLKGSFDKI GIEWEEFHAG
KYKSAPETLT RENMSQVNRE AKTLLINDIF DELVSAIAEA RGMTESTVKE IIDNGPYLVI
DEALEAGLID QINYESDLLE KIGGEDDEYE TVSGKDYMRE CEFPSSGKKF ALIFAVGEIV
SGDGTSGQFV GSKSMTRWIR EAAEDEETKA ILIRVDSPGG SALASDIIWR EIIQAREKKP
IVVSMGDLAA SGGYYISAPA NYIFAEPTTI TGSIGVFGIR PVMGNLFKMI GANTETILKG
KNSNLFDSSK LMSPEQRSIV EKSINQTYDT FLERVSEGRS MDYDDVHAVA QGRVWTGNQA
LERGLVDDIG DLTAAVEKAK ELAEIDNDQQ VWLDVYPRKK DLFEILREKD FPFASTKKYG
MLPKELQKAA EIYHWQKLYR PEEPLARLPY IITAE
//
