HTOA_HAEIN
ID HTOA_HAEIN Reviewed; 466 AA.
AC P45129;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable periplasmic serine protease do/HhoA-like;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN OrderedLocusNames=HI_1259;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; L42023; AAC22906.1; -; Genomic_DNA.
DR PIR; A64113; A64113.
DR RefSeq; NP_439414.1; NC_000907.1.
DR RefSeq; WP_005694316.1; NC_000907.1.
DR AlphaFoldDB; P45129; -.
DR SMR; P45129; -.
DR STRING; 71421.HI_1259; -.
DR EnsemblBacteria; AAC22906; AAC22906; HI_1259.
DR KEGG; hin:HI_1259; -.
DR PATRIC; fig|71421.8.peg.1311; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_6; -.
DR OMA; IIGINRQ; -.
DR PhylomeDB; P45129; -.
DR BioCyc; HINF71421:G1GJ1-1287-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 2.
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 Pfam; PF00595; PDZ; 2.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR TIGRFAMs; TIGR02037; degP_htrA_DO; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 3: Inferred from homology;
KW Hydrolase; Periplasm; Protease; Reference proteome; Repeat;
KW Serine protease; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..466
FT /note="Probable periplasmic serine protease do/HhoA-like"
FT /id="PRO_0000026936"
FT DOMAIN 270..361
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 367..458
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
SQ SEQUENCE 466 AA; 49434 MW; ED050A00047B5851 CRC64;
MKKTRFVLNS IALGLSVLST SFVAHVAQAT LPSFVSEQNS LAPMLEKVQP AVVTLSVEGK
AKVDSRSPFL DDIPEEFKFF FGDRFAEQFG GRGESKRNFR GLGSGVIINA SKGYVLTNNH
VIDGADKITV QLQDGREFKA KLVGKDEQSD IALVQLEKPS NLTEIKFADS DKLRVGDFTV
AIGNPFGLGQ TVTSGIVSAL GRSTGSDSGT YENYIQTDAA VNRGNSGGAL VNLNGELIGI
NTAIISPSGG NAGIAFAIPS NQASNLVQQI LEFGQVRRGL LGIKGGELNA DLAKAFNVSA
QQGAFVSEVL PKSAAEKAGL KAGDIITAMN GQKISSFAEI RAKIATTGAG KEISLTYLRD
GKSHDVKMKL QADDSSQLSS KTELPALDGA TLKDYDAKGV KGIEITKIQP NSLAAQRGLK
SGDIIIGINR QMIENIRELN KVLETEPSAV ALNILRGDSN FYLLVQ