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Database: UniProt
Entry: A0A023D378_ACIMT
LinkDB: A0A023D378_ACIMT
Original site: A0A023D378_ACIMT 
ID   A0A023D378_ACIMT        Unreviewed;       518 AA.
AC   A0A023D378;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE            EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
DE   AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN   ORFNames=Amme_016_029 {ECO:0000313|EMBL:GAJ28246.1};
OS   Acidomonas methanolica NBRC 104435.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidomonas.
OX   NCBI_TaxID=1231351 {ECO:0000313|EMBL:GAJ28246.1, ECO:0000313|Proteomes:UP000019760};
RN   [1] {ECO:0000313|Proteomes:UP000019760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB58 {ECO:0000313|Proteomes:UP000019760};
RX   PubMed=24330138; DOI=10.1111/1574-6968.12357;
RA   Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA   Matsushita K., Azuma Y.;
RT   "Draft Genomic DNA Sequence of the Facultatively Methylotrophic Bacterium
RT   Acidomonas methanolica type strain MB58.";
RL   FEMS Microbiol. Lett. 351:9-13(2014).
RN   [2] {ECO:0000313|EMBL:GAJ28246.1, ECO:0000313|Proteomes:UP000019760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB58 {ECO:0000313|EMBL:GAJ28246.1,
RC   ECO:0000313|Proteomes:UP000019760};
RA   Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA   Matsushita K., Azuma Y.;
RT   "Draft genomic DNA sequence of the facultatively methylotrophic bacterium
RT   Acidomonas methanolica type strain MB58.";
RL   FEMS Microbiol. Lett. 351:9-13(2014).
CC   -!- FUNCTION: Might be efficient in the degradation of transiently
CC       denatured and unfolded proteins which accumulate in the periplasm
CC       following stress conditions. {ECO:0000256|ARBA:ARBA00002610}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Acts on substrates that are at least partially unfolded. The
CC         cleavage site P1 residue is normally between a pair of hydrophobic
CC         residues, such as Val-|-Val.; EC=3.4.21.107;
CC         Evidence={ECO:0000256|ARBA:ARBA00001772};
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:GAJ28246.1}.
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DR   EMBL; BAND01000016; GAJ28246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A023D378; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000019760; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00987; PDZ_serine_protease; 2.
DR   Gene3D; 2.30.42.10; -; 2.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011782; Pept_S1C_Do.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR   PANTHER; PTHR22939:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR   PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..518
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038485876"
FT   DOMAIN          295..371
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          423..479
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          72..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        147
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        177
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        251
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ   SEQUENCE   518 AA;  54335 MW;  3636CBB305DCAC64 CRC64;
     MTQHSLPRRL SMITLCGATV LSSPLVSSPA VAEGETPAAA PPVVSASRPV PESFADLAAR
     LLPAVVNVSI SATLKPGDGD DDDDDGPDGS PGDGPQIPEF PPGSPMEKFF HDFMNRKPSP
     DAPPRKMQAL GSGFIISPDG YIVTNNHVVK DADQVSVTLQ DDTVLKARIV GRDSRTDLAV
     IKVDAPHPLP TVAFGNSDAA RVGDWVLAIG NPFGLSGTVT AGIVSSRGRS IEHDAYDDFI
     QTDAPINRGN SGGPLFNLKG EVIGINTAIY SPSGGSIGIG FSIPSNDARG VIEQLRNLGH
     VQRGWLGVRV QDVTHDIAES LGLPSLKGAM VAGIESKSPA EEAGIKPGDV INKLNGEAVD
     GKSLPRLVAA IPPGSKAAFG IWRKGSALTL DVTLKPSPEA PDLPPTAPRK DETAKKTIKL
     ADLGLTLGMI DDAARQKYHL TDSQRGVLVT AVAPDSPAAE RGLEAGNLVT EVQQVEVDSP
     EALSREIDRA RDAKRHSVLL LVQDSDGMRW VPLPLDKS
//
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