LONH_HAEIN
ID LONH_HAEIN Reviewed; 601 AA.
AC P43865;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Putative Lon protease homolog;
DE EC=3.4.21.-;
DE AltName: Full=ATP-dependent protease La homolog;
GN OrderedLocusNames=HI_1324;
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 -!- DOMAIN: Lacks the ATP-binding domain.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; L42023; AAC22971.1; -; Genomic_DNA.
DR PIR; F64116; F64116.
DR RefSeq; NP_439475.1; NC_000907.1.
DR AlphaFoldDB; P43865; -.
DR SMR; P43865; -.
DR STRING; 71421.HI_1324; -.
DR MEROPS; S16.A10; -.
DR EnsemblBacteria; AAC22971; AAC22971; HI_1324.
DR KEGG; hin:HI_1324; -.
DR PATRIC; fig|71421.8.peg.1376; -.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_014785_2_0_6; -.
DR OMA; GFFTICQ; -.
DR PhylomeDB; P43865; -.
DR BioCyc; HINF71421:G1GJ1-1349-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..601
FT /note="Putative Lon protease homolog"
FT /id="PRO_0000076149"
FT DOMAIN 363..560
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10087"
FT ACT_SITE 498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10087"
SQ SEQUENCE 601 AA; 67570 MW; 14B8DB4941DF49F5 CRC64;
MVNFSRKRPA VSSLFSQQQA IEQSLNWQAL QPDLVIQDFP LEPVNFWALQ PNATQGIDLF
LRHPTRSLLM MKVGEPVEYA ELLQNFISQN HHKVRSIFGV NYVIEQGDSF SFPHVYTEPA
KSLDDNFASQ GEALSALYCD QFQLFGSFRI HPRSQDIQLV PGLVHKANGG VLILSAATLL
SQFDLWGRLK QILQTQTFDW YSAHPFKNLP CDIPSYALNL KVIVLGNRTE LATLAELEEN
LYSFADYAEI ESYISVAEVE EQKTWAGYVQ QMAQEQNIEL DFLALNKLYQ LLVRESENRF
LINASPLKLK EILQDASTFT EKTALSAVDF EGIFQQKLAQ YGFLKEQTYA DILNEQVYVE
TQGEIVGQIN GLSVIEYPGT PVCFGEPSRI SCIVQFGDGE VIDVERKNEL AGNIHGKGMM
IAQACLSNIL DLPSQLPFSA SLVFEQSYGE IDGDSASLAI FCVLVSALAD LPLPQHIAIT
GSIDQFGLVH SVGGVNDKIE GFFTICQRRG LTGKQGVIIP MTTIQQLSLS DDVKSAVKNG
EFFIYPVEDI YQACELLFGR DLLDENKDYT EKTESLSRLI QRRIEGRADS ERKSFWHFFR
S