ID A0A0M4GYY2_9GAMM Unreviewed; 460 AA.
AC A0A0M4GYY2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AMQ28_02960 {ECO:0000313|EMBL:ALD03444.1};
OS Acinetobacter sp. TTH0-4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1646498 {ECO:0000313|EMBL:ALD03444.1, ECO:0000313|Proteomes:UP000055186};
RN [1] {ECO:0000313|EMBL:ALD03444.1, ECO:0000313|Proteomes:UP000055186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTH0-4 {ECO:0000313|EMBL:ALD03444.1,
RC ECO:0000313|Proteomes:UP000055186};
RA Zhang G.;
RT "Acinetobacter qinghaiensis sp. nov., isolated from active layer of
RT permafrost region.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP012608; ALD03444.1; -; Genomic_DNA.
DR RefSeq; WP_053580234.1; NZ_CP012608.1.
DR AlphaFoldDB; A0A0M4GYY2; -.
DR STRING; 1646498.AMQ28_02960; -.
DR KEGG; att:AMQ28_02960; -.
DR PATRIC; fig|1646498.3.peg.609; -.
DR Proteomes; UP000055186; 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; 2.
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:ALD03444.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..460
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039442028"
FT DOMAIN 247..341
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 360..438
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 103
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 460 AA; 49644 MW; B9A488B20AF6A15B CRC64;
MKNSYLTKGV FATVFTLASI QTYAASPVDF SNLVAQVSPA VVSVNVVKKM TQEELLQQQV
PEILRRFFGN QVIIPQQQAP QEKTGYGSAF FISKDGYLLT NHHVVEDASK VTIMLNDRRE
IDATVVGSDE RTDVALLKVN GSNFPELKTG NVDQLRVGEP VLAIGSPFGF DYSASAGIVS
AKMRNMMGET SVPFIQTDVA LNPGNSGGPL FNQRGEVVGV NSRIFSGTGG YMGLSFSIPI
DVAMDVADQL KRNGKVTRSY LGVMLQDIDR NLAESYRLDK PEGALVTEVA PNSPAAKAGL
QTGDVILKYN GSAISRTSDL LNYLNRTSPN QVIQLQILRD DKTRNISATL TLAPDDTPAK
VEQNAKNNGP VLGVSIRNLT AAEQSQLEVK GGIFIQEVKR EGIAAQARIT AGDVITQVNN
KVILNSVDFV KAASELKKGT VARVSIIRQG QRAIVGMRIE
//
