ID D9QQ40_ACEAZ Unreviewed; 391 AA.
AC D9QQ40;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=HtrA2 peptidase {ECO:0000313|EMBL:ADL12631.1};
DE EC=3.4.21.108 {ECO:0000313|EMBL:ADL12631.1};
GN OrderedLocusNames=Acear_1108 {ECO:0000313|EMBL:ADL12631.1};
OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Acetohalobium.
OX NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL12631.1, ECO:0000313|Proteomes:UP000001661};
RN [1] {ECO:0000313|EMBL:ADL12631.1, ECO:0000313|Proteomes:UP000001661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC {ECO:0000313|Proteomes:UP000001661};
RX PubMed=21304692;
RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT 7288).";
RL Stand. Genomic Sci. 3:57-65(2010).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP002105; ADL12631.1; -; Genomic_DNA.
DR RefSeq; WP_013278077.1; NC_014378.1.
DR AlphaFoldDB; D9QQ40; -.
DR STRING; 574087.Acear_1108; -.
DR KEGG; aar:Acear_1108; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_2_9; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000001661; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADL12631.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001661};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 281..361
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 391 AA; 43024 MW; D56A1DD5FA348A35 CRC64;
MWNNIAVSRK SLIKYLAVIM IGIVVSGGLF IGLSTGQAFA QNEADSTQNV YKSNFFADIA
SKVDAAVVRI NVKVEIDSEK LKENYPFFND PYFKKFFEQQ IPFEGEGNPK FRQGFGTGFI
ISQDGYILTN EHVIHGAEEV TVKLSDRKEP IKAEVVGTDF SLDLAVLKIN VNDKLPAVKL
GNSDNIKPGD WTVAIGNPYG LNHTVTVGVI SALGRPLRIR QGKKPRVYKN MIQTDAAINP
GNSGGPLLNR EGQVIGINTA INAQAQGIGF AIPINEAKRV LSDLKQHGKV IRPWMGVYMQ
PITEEMTEYF NLESTEGALI ADIISDSPAD KAGLKAGDVI VEINEIAVEN PEDVVKLVEK
AEVGDKMVLR VLREGYKRFV SVTLDERPKE Y
//
