ID S3NAV0_9GAMM Unreviewed; 340 AA.
AC S3NAV0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Signal peptide peptidase SppA, 36K type {ECO:0000313|EMBL:EPF71499.1};
GN ORFNames=F945_02528 {ECO:0000313|EMBL:EPF71499.1};
OS Acinetobacter rudis CIP 110305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF71499.1, ECO:0000313|Proteomes:UP000014568};
RN [1] {ECO:0000313|EMBL:EPF71499.1, ECO:0000313|Proteomes:UP000014568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF71499.1,
RC ECO:0000313|Proteomes:UP000014568};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL Submitted (JUN-2013) 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:EPF71499.1}.
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DR EMBL; ATGI01000032; EPF71499.1; -; Genomic_DNA.
DR RefSeq; WP_016656928.1; NZ_KE340353.1.
DR AlphaFoldDB; S3NAV0; -.
DR STRING; 632955.GCA_000829675_01743; -.
DR PATRIC; fig|421052.3.peg.2472; -.
DR eggNOG; COG0616; Bacteria.
DR HOGENOM; CLU_046540_1_1_6; -.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000014568; 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:0006508; P:proteolysis; IEA:InterPro.
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; IPR004635; Pept_S49_SppA.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047272; S49_SppA_C.
DR NCBIfam; TIGR00706; SppA_dom; 1.
DR PANTHER; PTHR42987; PEPTIDASE S49; 1.
DR PANTHER; PTHR42987:SF4; PROTEASE SLR0021-RELATED; 1.
DR Pfam; PF01343; Peptidase_S49; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000014568};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 148..299
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 37228 MW; 96EAD98AFCB64AE8 CRC64;
MSDWPPQPHK EKTDQPATPT GQEWKILEKA VLSSVKEQQR SRRWGIFFKF VSMLYVLAIL
IFMFRGCTLT SSTENVTGIT DTHLAVVNII GTIDSGNQSV NSIDTIKSLK SAFEAKGSRA
VVLNINSPGG SPVQSDDIWQ EIQYLKKQHP NKKVYAVIGD MGASGAYYIA SAADQIWVNP
SSLVGSIGVI MPNYGVSGLA QKLGIEDRTM TAGSNKDILS MSKPINAEQK QHIQALLDNV
HSHFIQAVKT GRGDKLKSTD PAIFSGLFWT GEQAIKLGIA DKAGNLESLK RELDISKTVN
YTVERTPFDS IMGRMGSEMG QHLGTAVMQQ VQSQNQTKIQ
//
