ID V2T5W7_9GAMM Unreviewed; 343 AA.
AC V2T5W7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Signal peptide peptidase SppA, 36K type {ECO:0000313|EMBL:ESK37838.1};
GN ORFNames=P256_02274 {ECO:0000313|EMBL:ESK37838.1};
OS Acinetobacter nectaris CIP 110549.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1392540 {ECO:0000313|EMBL:ESK37838.1, ECO:0000313|Proteomes:UP000023785};
RN [1] {ECO:0000313|EMBL:ESK37838.1, ECO:0000313|Proteomes:UP000023785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110549 {ECO:0000313|EMBL:ESK37838.1,
RC ECO:0000313|Proteomes:UP000023785};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter nectaris CIP 110549.";
RL Submitted (OCT-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:ESK37838.1}.
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DR EMBL; AYER01000009; ESK37838.1; -; Genomic_DNA.
DR RefSeq; WP_023273884.1; NZ_KI530735.1.
DR AlphaFoldDB; V2T5W7; -.
DR PATRIC; fig|1392540.3.peg.2195; -.
DR eggNOG; COG0616; Bacteria.
DR HOGENOM; CLU_046540_1_1_6; -.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000023785; 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:UP000023785};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..302
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 37430 MW; A7E3682726DA2BEC CRC64;
MSDWPPKPTD QAMNNQSNSQ REQKGNEWEL LEKVVLSSIN EQKKTRKWGI FFKSLTFIFL
FIVLFLLVKS CSISKDMDSE KSVGDHLAIV DIQGTIGSST KDVNSADTIK ALKAAFKAEN
SKAIVLNINS PGGSPVESDN IWQEIRYLEK EHPNKKVYAV IGDMGASGAY YIASAVNEIW
VNPSSLVGSI GVIMPNYGVA GLAQKLGVED RTMTSGANKD ILSMTKPINP AQREHVQAVL
DDVHQHFIDA VKEGRGDRLK NADPSVFSGL FWSGSQAIKL GIADHAGNLE SLKRTLKISK
TVDYTVEHNP LESILGKMGA EMGQGLGASL TQQLEAKQQA SLQ
//
