ID   A0A1Q2CKK7_9ACTN        Unreviewed;       406 AA.
AC   A0A1Q2CKK7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Peptidase S49 domain-containing protein {ECO:0000259|Pfam:PF01343};
GN   ORFNames=BW730_02645 {ECO:0000313|EMBL:AQP46595.1};
OS   Tessaracoccus aquimaris.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=1332264 {ECO:0000313|EMBL:AQP46595.1, ECO:0000313|Proteomes:UP000188145};
RN   [1] {ECO:0000313|Proteomes:UP000188145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSG39 {ECO:0000313|Proteomes:UP000188145};
RA   Tak E.J., Bae J.-W.;
RT   "Tessaracoccus aquaemaris sp. nov., isolated from the intestine of a Korean
RT   rockfish, Sebastes schlegelii, in a marine aquaculture pond.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S49 family.
CC       {ECO:0000256|ARBA:ARBA00008683}.
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DR   EMBL; CP019606; AQP46595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2CKK7; -.
DR   STRING; 1332264.BW730_02645; -.
DR   KEGG; tes:BW730_02645; -.
DR   OrthoDB; 5623708at2; -.
DR   Proteomes; UP000188145; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000188145};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        56..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          180..342
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..44
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   406 AA;  42216 MW;  E3D3B9012618C2E8 CRC64;
     MDNDPDLTSF PPPHPRDQRV DHVDAPQPRP QPANPGPPPP VATLDRKPQG TFARGFGWGT
     GIATGVAVVG TALSLLSLIG LWAMAAALLA TGGQPSEQTT VVWGSGSERL RAIEISGAIM
     AESSDGSLLS AGTYGYEVAR ELDGLSKDDG AGVVLLVNTP GGSIAGSKAI SDAIERYQER
     TGQKVLVHVS SMSASGGVYS TAPADEIIAD YGSLVGSIGV IFGPFTHYQD VTGTTGTLLE
     SGVTTTGGVT QEYLSQGTGK DFGNPFRAMT EREREVYMGG LEREYDAFVA HVAEHRGIPA
     KTIVDDLGAF MFDPVTAQEK KLIDSVMGRE EFFRHAAETA GLNPDDTRVE ALSAPSGLET
     LLGVERRLGL APAADQGNGV TPVLSQAICG GIQPLALAGD VRALCG
//