ID A0A1W9HK67_9PROT Unreviewed; 623 AA.
AC A0A1W9HK67;
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:OQW47849.1};
GN ORFNames=A4S16_07525 {ECO:0000313|EMBL:OQW47849.1};
OS Proteobacteria bacterium SG_bin6.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1827383 {ECO:0000313|EMBL:OQW47849.1, ECO:0000313|Proteomes:UP000192863};
RN [1] {ECO:0000313|EMBL:OQW47849.1, ECO:0000313|Proteomes:UP000192863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG_bin6 {ECO:0000313|EMBL:OQW47849.1};
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:OQW47849.1}.
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DR EMBL; LWDJ01000006; OQW47849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9HK67; -.
DR Proteomes; UP000192863; 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; IPR002142; Peptidase_S49.
DR InterPro; IPR047217; S49_SppA_67K_type_N.
DR InterPro; IPR047272; S49_SppA_C.
DR NCBIfam; TIGR00705; SppA_67K; 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|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..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..275
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 373..524
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 390
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 623 AA; 65684 MW; 8ED425AE60BBC47E CRC64;
MKLLRGAWKL LVGIKDALVL IAMLLFFGGL FTALAFRPNP AAIKDGALVI ALDGPIVEQP
AGPQFDFGGG GEPAELRLRD VVRAIRAAKD DAHVKALVLD FDSFGGGLPA ALNEVGAAVE
SVRKSGKPVL AYATAYSDAS YRIASHASEI WMHPMGGTLF TGPGGSQLYY KGLLDKLGVN
VHVYRVGKFK SFIEPFTRSD QSPEARENSV ALYTAIGNDW RQQVGQARPK AQAAAFLDQA
TQRVLAAGGD IAQANKAAGL IDKLGDRMAF NARVAEIAGA APAGKGVFKR IRYKDFLAAH
PLPTGGDAIG VLTVAGDIID GKADAGTAGG DTIARLLNDG IETKKLKALV VRVDSPGGSA
LASEVIRQAI LRAKAKGLPV VVSMGGVAAS GGYWVSTAGD TIFAEPSTIT GSIGIFGVVP
SFENSLAKLG IATDGVKTTP LSGQPDIAGG FSPEVDQLFQ AGIEHGYRQF LERVAQARRK
SVQQVDEIAQ GRVWDGGTAR QIGLVDRFGG IDDAIAEAAR RAKLDPANVH AEYLEKKPDW
WAEFFNSFAR KNDEDEANAS GDAYAQIAAQ RRAVFARAVG DARRLATGAA VQARCLECAG
LAPARLDAED RKLITLLFAK LAR
//
