ID B7J9J7_ACIF2 Unreviewed; 479 AA.
AC B7J9J7;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Serine protease, DO/DeqQ family {ECO:0000313|EMBL:ACK80869.1};
GN OrderedLocusNames=AFE_1396 {ECO:0000313|EMBL:ACK80869.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK80869.1, ECO:0000313|Proteomes:UP000001362};
RN [1] {ECO:0000313|EMBL:ACK80869.1, ECO:0000313|Proteomes:UP000001362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC {ECO:0000313|Proteomes:UP000001362};
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II.,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; CP001219; ACK80869.1; -; Genomic_DNA.
DR AlphaFoldDB; B7J9J7; -.
DR SMR; B7J9J7; -.
DR STRING; 243159.AFE_1396; -.
DR MEROPS; S01.453; -.
DR PaxDb; 243159-AFE_1396; -.
DR KEGG; afr:AFE_1396; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_6; -.
DR Proteomes; UP000001362; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; IPR041489; PDZ_6.
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; PF13180; PDZ_2; 1.
DR Pfam; PF17820; PDZ_6; 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:ACK80869.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001362};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..479
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039241914"
FT DOMAIN 262..327
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 479 AA; 49673 MW; 7F2FD2CFA629B02D CRC64;
MALCMGLGLS IGAMTPAWAD SGASGQALVG LPDFTPIVKQ YGPAVVNIST TETRVARGVT
SPFPPNSPLN QFFAPFFGAP GQPGAPGGGA GQKYQVQSLG SGFVISSDGY IVTAAHVVKG
AQKIIVSLTN HHQYAAHLVG LSARMDVALL KIDAKNLPVV QIGDSSKLEV GQWVLAVGSP
FGFENSVTQG VISATSRPLP DDPYIPFVQT DVPINPGNSG GPLFNMRGQV IGINDQIYTN
SGGYMGLSFS IPINVAMDAV KQLKLHQKVH FGWLGVMIQD VSMDLAKSFH MKEPVGALVS
QVVPDGPAAK AGLRPGDVIV SFDGQAIYNS GQLPPLVGVL PAGFKAKLGV IRDGKPMSLN
IVVESLPGNL ENTVESAASG GPAQEGEVKR LNVQVGPLTA EARKQLHVNT GVLVLGVGVG
PAAEAGIRPG DVILQVAQQQ ITNAADLQKL VAALPAGQPI PVLVRRGEGS FYLVLSLPH
//
