ID A0A1W9K8K5_9PROT Unreviewed; 624 AA.
AC A0A1W9K8K5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Signal peptide peptidase SppA {ECO:0000313|EMBL:OQW80497.1};
GN ORFNames=BVN32_01180 {ECO:0000313|EMBL:OQW80497.1};
OS Proteobacteria bacterium ST_bin14.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1978762 {ECO:0000313|EMBL:OQW80497.1, ECO:0000313|Proteomes:UP000192961};
RN [1] {ECO:0000313|EMBL:OQW80497.1, ECO:0000313|Proteomes:UP000192961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST_bin14 {ECO:0000313|EMBL:OQW80497.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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:OQW80497.1}.
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DR EMBL; MSXR01000001; OQW80497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9K8K5; -.
DR STRING; 1978762.BVN32_01180; -.
DR Proteomes; UP000192961; 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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..279
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 374..525
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 190
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 391
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 624 AA; 65470 MW; F36E87F98D618831 CRC64;
MKLVRGAWKL LVGIKDGLVL IAMLLFFGLL FAALSSKPNP GGVRDGALVL DLAGVIVEQP
AEAEFNFGGN DGPREIRLRD LVRVIDAAKD DKRVKAIVLD LDSFAGGYPA AVSEVATALG
RVRSSGKPVL AYATGYTDSG YRLAANASEI WMNPMGGTLF TGPGGSQLYY KGLIDKLGVN
VHVYRVGKFK SFVEPYTRSD QSPEARAASE ALYGSLLTDW KDAVGKARPK AQSAQFLATP
AAQIAATKGD IAAANLKAGL IDKLGDRAEF NQRVIALAGL KSGKGAPTFN AITYADFLKA
NPLPSTGDAI GVITVAGDIV DGKAGPGTAG GATISKLVLD GLAKKTLKAL VVRVDSPGGS
ALASEAIRRA VLEAKAQKLP VVISMGSIAA SGGYWVATAG DVIFAEPNTI TGSIGIFGII
PTFENSLKKL GITADGVKSS PLSGQPDVFS GTNSEVDSIL QAGIEHGYAQ FLSRVASARK
MSVEKVDSIA QGRVWDGGTA RQIGLVDRFG TLQDAIDEAA KRAKLDPTKV HAEYLEKKPG
WFARFANDFG RKDDDEEADQ PGDAFARIAR DRRAVFAQAL GDVRRLALGG SVQARCLECG
GLAPAAPDRD DLRLMDVVLA RLGL
//
