ID A0A1S1MWV3_9GAMM Unreviewed; 622 AA.
AC A0A1S1MWV3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Signal peptide peptidase SppA {ECO:0000313|EMBL:OHU91691.1};
GN ORFNames=BET10_10990 {ECO:0000313|EMBL:OHU91691.1};
OS Pseudoalteromonas amylolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1859457 {ECO:0000313|EMBL:OHU91691.1, ECO:0000313|Proteomes:UP000179786};
RN [1] {ECO:0000313|EMBL:OHU91691.1, ECO:0000313|Proteomes:UP000179786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JW1 {ECO:0000313|EMBL:OHU91691.1,
RC ECO:0000313|Proteomes:UP000179786};
RA Wu Y.-H., Cheng H., Jin X.-B., Wang C.-S., Xu X.-W.;
RT "Pseudoalteromonas amylolytica sp. nov., isolated from the surface
RT seawater.";
RL Submitted (SEP-2016) 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:OHU91691.1}.
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DR EMBL; MKJU01000025; OHU91691.1; -; Genomic_DNA.
DR RefSeq; WP_070985600.1; NZ_MKJU01000025.1.
DR AlphaFoldDB; A0A1S1MWV3; -.
DR STRING; 1859457.BET10_10990; -.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000179786; 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 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 132..292
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 389..539
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 200
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 406
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 622 AA; 68896 MW; CA143484ED925D52 CRC64;
MIGKFFKALW HGLNFSRRLV LNIIFFIIIV AAIIAIFSDK EEITVSENSV LRLNLNGYLV
EELTYIDPLD AAFQDLSESG DEPHEILLDD VLEVINRAKK DDRIQVLWLD LENLYGGHLD
KLEVITQALD EFKNADKKVI AHGSYYSQAQ YYLAAHADTI SLHPYGSVKI RGFSSYPLYF
KDALDKLKVT QHIFRVGTYK SAIEPLIRND MSDAAKEANR LWLGELWQQY KQEIADARPF
GLDNFDETLD DYEMKIQAVK GDFAQYALHN GWVDELKTDQ QLQSELIELV GLDKRGKTFN
QISFDEYLEM IKPPVQFENP ITEKVAVIVA RGAIVDGKQK AGKIGGDSTA ALLKRARLND
KVKAVVLRID SGGGSMFASE TIRNEILAIK AAGKPVVASM GSVAASGGYW IAASTNEIWA
APSTITGSIG VFGAILTFEN SLKELGIHSD GVATTELNGM SIARGIDKQL VDIYQLSVEN
SYDKFISLVA QERNMTKEAV DKVAQGRVWT ATQAKEFGLI DNLGYKKDAI EAAAKLANLD
FYEVITIEQE LSEKEQLIRE FLGSATVKSA LAGVAPDASV AKLASGYLSP ITSQVEQNLD
LLNQFNDPNG TYVRCLVCEV SF
//
