ID G1XYL9_9PROT Unreviewed; 500 AA.
AC G1XYL9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=AZA_28798 {ECO:0000313|EMBL:EGY01644.1};
OS Nitrospirillum amazonense Y2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Nitrospirillum.
OX NCBI_TaxID=1003237 {ECO:0000313|EMBL:EGY01644.1, ECO:0000313|Proteomes:UP000018435};
RN [1] {ECO:0000313|EMBL:EGY01644.1, ECO:0000313|Proteomes:UP000018435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y2 (ATCC 35120) {ECO:0000313|Proteomes:UP000018435};
RX PubMed=21838888; DOI=10.1186/1471-2164-12-409;
RA Sant'anna F.H., Almeida L.G., Cecagno R., Reolon L.A., Siqueira F.M.,
RA Machado M.R., Vasconcelos A.T., Schrank I.S.;
RT "Genomic insights into the versatility of the plant growth-promoting
RT bacterium Azospirillum amazonense.";
RL BMC Genomics 12:409-409(2011).
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:EGY01644.1}.
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DR EMBL; AFBX01000292; EGY01644.1; -; Genomic_DNA.
DR RefSeq; WP_004272463.1; NZ_AFBX01000292.1.
DR AlphaFoldDB; G1XYL9; -.
DR PATRIC; fig|1003237.3.peg.1832; -.
DR Proteomes; UP000018435; 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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EGY01644.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018435};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..500
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038452387"
FT DOMAIN 287..345
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 378..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 500 AA; 51739 MW; 41A04466E0EEB40F CRC64;
MTSLPTVRTA KKRFPRLAVT ALAIGLMTGT ALVAPPAAIT AHAASPASLP SFADLVEKVT
PAVVTITAAH KVTTPQVPQE LQEMMRHFGL PDEALPGGGG RGGNGRPRIE SALGSGFVID
PSGYIVTNRH VIEGADEVKV HFQDQTDDVP AKIVGQDERS DLALLKVEPK KPLQALAFGD
SDKMRPGDWV IAVGNPFGLG GTVTAGIVSA RGRDIDAANL NDFLQIDASI NKGNSGGPTF
NANGEVIGIN TAIFSPTGGS VGIGFAIPSN VAKPVIEKLK ATGHVQRGYL GVTLQAVTPE
IADSLGLKEP KGAIINAVSP KSPAEKGGLK QGDVVQSING KSIDNQRDLA RNVAGIDPGK
TVDLGVLRGG KAITVSVKLG EAPNSGDKDN GPGGSTSPDG KGDNTSVAGL KLGKLDDRTR
ERMGLDNDIQ GVVIVDPGKD ELGLRPGDII ASVNNESVKA PADVNNQVEK AKKDGRKSVL
LLVRRGDQQM FLPLPVTPKG
//
