ID A0A1E5E249_9VIBR Unreviewed; 457 AA.
AC A0A1E5E249;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Serine endoprotease DegQ {ECO:0000313|EMBL:OEF25490.1};
GN ORFNames=A1QC_08965 {ECO:0000313|EMBL:OEF25490.1};
OS Vibrio rumoiensis 1S-45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1188252 {ECO:0000313|EMBL:OEF25490.1, ECO:0000313|Proteomes:UP000094070};
RN [1] {ECO:0000313|EMBL:OEF25490.1, ECO:0000313|Proteomes:UP000094070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1S-45 {ECO:0000313|EMBL:OEF25490.1,
RC ECO:0000313|Proteomes:UP000094070};
RX PubMed=22955834; DOI=10.1126/science.1219385;
RA Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA Le Roux F., Mincer T., Polz M.F.;
RT "Ecological populations of bacteria act as socially cohesive units of
RT antibiotic production and resistance.";
RL Science 337:1228-1231(2012).
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:OEF25490.1}.
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DR EMBL; AJYK02000062; OEF25490.1; -; Genomic_DNA.
DR RefSeq; WP_017024947.1; NZ_AJYK02000062.1.
DR AlphaFoldDB; A0A1E5E249; -.
DR STRING; 1188252.A1QC_08965; -.
DR eggNOG; COG0265; Bacteria.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000094070; 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; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF00595; PDZ; 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:OEF25490.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094070};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..457
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038489362"
FT DOMAIN 260..351
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 363..449
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 457 AA; 47848 MW; E590B6D1C1073331 CRC64;
MKGPLLVLSA VSLSLSAILT PVSASATIPN SVNGQEMPSL APMLAKVTPA VVTVSVEGKK
TSNAQSIPEQ FRYFFGPDIP VQSLPERQFK GLGSGVIIDA KNGYIVTNYH VINDADKIQV
TLSDKREFNA TLIGGDKLSD IALIKLDKKI SGLTQATLAD SDHLRVGDFA VAIGNPFGLG
QTVTSGIISA LGRSGLNIEN FENFIQTDAA INTGNSGGAL VNLNGELVGI NTAILGPNGG
NVGIGFAIPS NMVKNLTEQI IEFGEVKRGI LGVQGGEITP DLAEAMGYSS SKGAFVSQVM
PDSAAEKAGL KAGDVITSIN GKEIATFGEL RAKIATIGAG KEVELGLLRD GKAITADVTL
GEMQQLQASA EELHPGLEGA QFSNTNSSDA ISGIKITDVA KGSPAESYQL KQDDIIIGVN
RTRVKNLAQM KKVLEHKTNI LALNIQRGDR TIYLVVK
//
