ID D1ATT1_ANACI Unreviewed; 484 AA.
AC D1ATT1;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=ACIS_00293 {ECO:0000313|EMBL:ACZ48959.1};
OS Anaplasma centrale (strain Israel) (Anaplasma marginale subsp. centrale
OS (strain Israel)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=574556 {ECO:0000313|EMBL:ACZ48959.1, ECO:0000313|Proteomes:UP000000630};
RN [1] {ECO:0000313|EMBL:ACZ48959.1, ECO:0000313|Proteomes:UP000000630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Israel {ECO:0000313|EMBL:ACZ48959.1,
RC ECO:0000313|Proteomes:UP000000630};
RX PubMed=19854912; DOI=10.1128/JB.01330-09;
RA Herndon D.R., Palmer G.H., Shkap V., Knowles D.P. Jr., Brayton K.A.;
RT "Complete genome sequence of Anaplasma marginale subsp. centrale.";
RL J. Bacteriol. 192:379-380(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001759; ACZ48959.1; -; Genomic_DNA.
DR RefSeq; WP_012880439.1; NC_013532.1.
DR AlphaFoldDB; D1ATT1; -.
DR STRING; 574556.ACIS_00293; -.
DR KEGG; acn:ACIS_00293; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_5; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000000630; Chromosome.
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, ECO:0000313|EMBL:ACZ48959.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..484
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039308186"
FT DOMAIN 264..369
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 364..441
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 118
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 484 AA; 50750 MW; 7F674B409AA6B4E4 CRC64;
MKRFLSLFLL IASLYSWALP SAAQSKVVVP DSRKGFSELA ARLLPAVVNI STEQTVDGDA
SSMGGQGFRF PGIPKGIFEE FFNNLEPLLV DPPKPRKVVS LGSGFIVDKS GLIVTNYHVI
ANAKEIHVKF SDNSTAKATV LGKDPKTDLA VLKVKTKKDL QPVTLGNSDD VLVGEWVLAI
GNPFGLGGSV SVGIISGRAR DINIGTASEF LQTDAAINRG HSGGPLFNAD GEVIGINTAI
MSPQGGGNVG VAFAIPSNNA ARVISVLSKG GRVEHGWLGV VIQHVTDDMT DSLGLERARG
ALISGVAKDS PAEKAGLKVG DVILEFNGQK IENMPQLTHL ITKAAVNEKA KVTVQRDGRT
LNVVVTIGKL PDDAVPGGAD QEATDDSIGI TVGSLPKSSK KQQQEGVLIL RVDHRSDAFS
EGVRKGDILL GINSTTINSV SDFSKEMGKI KGSSGGKGSL LLLVKKGGGD APPIYIPVKF
NKNA
//
