ID   A0A2A5CLW5_9GAMM        Unreviewed;       352 AA.
AC   A0A2A5CLW5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=S49 family peptidase {ECO:0000313|EMBL:PCJ44874.1};
GN   ORFNames=COA99_06395 {ECO:0000313|EMBL:PCJ44874.1};
OS   Moraxellaceae bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae.
OX   NCBI_TaxID=1889775 {ECO:0000313|EMBL:PCJ44874.1, ECO:0000313|Proteomes:UP000218379};
RN   [1] {ECO:0000313|Proteomes:UP000218379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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:PCJ44874.1}.
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DR   EMBL; NVVG01000045; PCJ44874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5CLW5; -.
DR   Proteomes; UP000218379; 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; IPR002142; Peptidase_S49.
DR   InterPro; IPR047272; S49_SppA_C.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        67..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          168..303
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  38369 MW;  75936D1144D8B88F CRC64;
     MEDESNNDVQ SQTNSRPTAG GDGQGRDNRR GGNKRGNPRR HGPSKEWKLV EQLALQSLEE
     QKKSRRWGIF FKFATLLYVI FIFVAFRSEA GGGDGAKSYE PHTALVDVVG IIMAGREAEA
     DVIVGGLRDA FEAKHSKAIL LRINSPGGSP VQSNMVYNEI MRLKEKYPEK KVYAAITDAG
     ASGAYFIAAA ADAIYADPAS IVGSIGVISD GFGFTKVMEK IGVERRVYSS GDNKAMLDPF
     SPLNAEQSAH FSSLLNNVHE QFIRAVRQGR GDRLKEDETI FSGLMWTGEQ ALELGLIDGL
     GSPGYVAREV VGVEEMVDYT QRPSPLQSIF DRIGVKIGIT IAESLGSNFS LR
//