ID H9UK83_SPIAZ Unreviewed; 608 AA.
AC H9UK83;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Trypsin-like serine protease with C-terminal PDZ domain {ECO:0000313|EMBL:AFG37926.1};
GN OrderedLocusNames=Spiaf_1871 {ECO:0000313|EMBL:AFG37926.1};
OS Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG37926.1, ECO:0000313|Proteomes:UP000007383};
RN [1] {ECO:0000313|Proteomes:UP000007383}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC {ECO:0000313|Proteomes:UP000007383};
RX PubMed=23991249; DOI=10.4056/sigs.3607108;
RA Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT Rift.";
RL Stand. Genomic Sci. 8:165-176(2013).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP003282; AFG37926.1; -; Genomic_DNA.
DR RefSeq; WP_014455909.1; NC_017098.1.
DR AlphaFoldDB; H9UK83; -.
DR STRING; 889378.Spiaf_1871; -.
DR MEROPS; S01.454; -.
DR KEGG; sfc:Spiaf_1871; -.
DR PATRIC; fig|889378.3.peg.1860; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_026857_0_0_12; -.
DR Proteomes; UP000007383; 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; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AFG37926.1};
KW Protease {ECO:0000313|EMBL:AFG37926.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007383}.
FT DOMAIN 404..486
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 608 AA; 67170 MW; D7D9F65E2098F6D3 CRC64;
MIHLTLFRRS NKLLLLLIAV AGIGCATVAE HSEPLPRASR AEQSVRELLE DREPQLALMY
LDSYRVRTAW DYPWQDELEL AAAEQLRELF EEAFDSGDHR TAGRLLRGLK LADPDYVDAG
EYQLQLARMA FETEYQEERF PLAIAAFLQL LQHDVGQLTD HTALLVQGME LIADQRDAFA
YETASERLQQ QGLSVADFID ELPVSPRPTA DQVPGVATIW VNKGIRLEDG VGRPDRMIGS
GFFIDERGYL VTNYHVIQSE VDPAYRGFSR AYIRPHDAPD SRIPAKVVGF DPVLDLALLK
VPYTPDYVFP VSGVRERSPG SRVYAIGSPG GLSNTITSGI ISAAGRRFFQ LGEAVQVDAP
LNPGNSGGPI LDEDGNLVGV VYAGIPQFDG ISFAVPSFWL RGILPQLYEE GRVQHPYLGI
SVHETHRGLE VVHVILGSPA DRAQLTVGDV VTGINGEAVT TLKDANRMLQ VAGPDSLVRL
SILREGDDGR RQDQQRLVTG SRPQRPLEAN LRGTSSFPES LFAPLYGVFL QPVRTGWFSS
DYTVERVLPG SIADEAGLSP QDPVTLQRWE YDEDRGIAAV VLRVRKRQSG YMDGAVMLPV
FIETTNVL
//
