GenomeNet

Database: UniProt
Entry: Q4QMI0
LinkDB: Q4QMI0
Original site: Q4QMI0 
ID   RAPA_HAEI8              Reviewed;         923 AA.
AC   Q4QMI0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   18-SEP-2019, entry version 91.
DE   RecName: Full=RNA polymerase-associated protein RapA {ECO:0000255|HAMAP-Rule:MF_01821};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01821};
DE   AltName: Full=ATP-dependent helicase HepA {ECO:0000255|HAMAP-Rule:MF_01821};
GN   Name=rapA {ECO:0000255|HAMAP-Rule:MF_01821};
GN   OrderedLocusNames=NTHI0873;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable
RT   Haemophilus influenzae: comparative study with H. influenzae serotype
RT   d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
CC   -!- FUNCTION: Transcription regulator that activates transcription by
CC       stimulating RNA polymerase (RNAP) recycling in case of stress
CC       conditions such as supercoiled DNA or high salt concentrations.
CC       Probably acts by releasing the RNAP, when it is trapped or
CC       immobilized on tightly supercoiled DNA. Does not activate
CC       transcription on linear DNA. Probably not involved in DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_01821}.
CC   -!- SUBUNIT: Interacts with the RNAP. Has a higher affinity for the
CC       core RNAP than for the holoenzyme. Its ATPase activity is
CC       stimulated by binding to RNAP. {ECO:0000255|HAMAP-Rule:MF_01821}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01821}.
DR   EMBL; CP000057; AAX87767.1; -; Genomic_DNA.
DR   RefSeq; WP_011272194.1; NC_007146.2.
DR   PRIDE; Q4QMI0; -.
DR   EnsemblBacteria; AAX87767; AAX87767; NTHI0873.
DR   KEGG; hit:NTHI0873; -.
DR   HOGENOM; HOG000218482; -.
DR   KO; K03580; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000002525; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   HAMAP; MF_01821; Helicase_RapA; 1.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR023949; Helicase_RapA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022737; RapA_C.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR040765; Tudor_1_RapA.
DR   InterPro; IPR040766; Tudor_2_RapA.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12137; RapA_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF18339; Tudor_1_RapA; 1.
DR   Pfam; PF18337; Tudor_RapA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; Complete proteome; DNA-binding; Helicase;
KW   Hydrolase; Nucleotide-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    923       RNA polymerase-associated protein RapA.
FT                                /FTId=PRO_1000088359.
FT   DOMAIN      162    332       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01821}.
FT   DOMAIN      443    597       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01821}.
FT   NP_BIND     175    182       ATP. {ECO:0000255|HAMAP-Rule:MF_01821}.
FT   MOTIF       278    281       DEAH box.
SQ   SEQUENCE   923 AA;  104415 MW;  637B44770A70D487 CRC64;
     MPFAIGQRWL SESENALGLG VITALDQRTV TIYFPAADET RIYAAAQAPL SRIVFSKGET
     LSHQAGWQGE ILDVQNMNGL LFYLVKTPQD EDVIVQERDI SPIISFSQAK DRLFSAQIDR
     SSHFALRYRT LCHQQAQFKS PLRGLRGTRA GLIPHQLHIA AEVGNRVNPR VLLADEVGLG
     KTIEAGMILQ NQLFAEKVQR VLIIVPETLQ HQWLVEMLRR FNLHFSLFDE ERCNDFDLDA
     VNPFMTESLI ICSLNWLETH PNRVEQALDA QFDCLIVDEA HHLVWSESAP SAAYLLVEQL
     ARIIPSVLLL TATPEQLGQE SHFARLRLLD PERFFDYQTF VKEQKRYQPV VNAIESLLAN
     KALSAVEKNH ISDLLLEQDV EPLFKAIASN NDEEQHRARQ ELIQALIDRH GTGRMLFRNT
     RQGVKGFPHR VYHQITLSEE NDKIDWLINF LKLHRDEKIF VICQTAATAI QLEQILRERE
     AIRAAVFHEK MSIIERDRAA AYFADLENGA QVLLSSSIGS EGRNFQFAAN LVLFDLPTNP
     DLLEQCIGRL DRIGQKRDVQ IYVPCAKDSP QIRLARWYNE GLNAFEQTCP MGMALFSQFE
     DELEKVRSNS TALSENEFSE LLKQTKTVRE KLKIELEKGR DRLLELNSNG GKQAQALADQ
     IADEDNSPEL VNFALKLFDI IGVEQEDLGA NSIVISPTGT MLVPDFPGLK EEGVTVTFDR
     ELALAREEME FLTWDHPMIR QGIDLVASGD IGKAAMALLV NKQLPAGTLL IELIYIVESQ
     SPKGLQLNRF LPPTPIRLLL DNKGNNIGEQ VAFETLHSKL KPLGKNIANQ MVKMARGNIE
     ALITRGDQLV KSLAEPIITE AKNQADQQLS AEINRLQALR AVNQNIRQSE IDILEQQRTQ
     SLDELSKANW RLDCLRVIVT NKE
//
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