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Database: UniProt
Entry: D2TJH2_CITRI
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Original site: D2TJH2_CITRI 
ID   D2TJH2_CITRI            Unreviewed;      1281 AA.
AC   D2TJH2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=ATP-dependent helicase HrpA {ECO:0000313|EMBL:CBG88388.1};
GN   Name=hrpA {ECO:0000313|EMBL:CBG88388.1};
GN   OrderedLocusNames=ROD_16271 {ECO:0000313|EMBL:CBG88388.1};
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG88388.1, ECO:0000313|Proteomes:UP000001889};
RN   [1] {ECO:0000313|EMBL:CBG88388.1, ECO:0000313|Proteomes:UP000001889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168 {ECO:0000313|EMBL:CBG88388.1,
RC   ECO:0000313|Proteomes:UP000001889};
RX   PubMed=19897651; DOI=10.1128/JB.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA   Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA   Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent evolution
RT   with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
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DR   EMBL; FN543502; CBG88388.1; -; Genomic_DNA.
DR   STRING; 637910.ROD_16271; -.
DR   KEGG; cro:ROD_16271; -.
DR   eggNOG; COG1643; Bacteria.
DR   HOGENOM; CLU_001832_3_3_6; -.
DR   Proteomes; UP000001889; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   CDD; cd17989; DEXHc_HrpA; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR024590; HrpA_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010222; RNA_helicase_HrpA.
DR   NCBIfam; TIGR01967; DEAH_box_HrpA; 1.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF11898; DUF3418; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:CBG88388.1};
KW   Hydrolase {ECO:0000313|EMBL:CBG88388.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          68..231
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          255..425
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1281 AA;  146495 MW;  FD7985BE85EFB8E2 CRC64;
     MLRDRQRFSR RLHGVKKVKN PDAQQAIYQE MAKEIEQAAG KVLLREAARP AIAYPENLPV
     SQKKQAILEA VRDHQVVIVA GETGSGKTTQ LPKICMELGR GVKGLIGHTQ PRRLAARTVA
     NRIAEELQTE PGGCIGYKVR FSDRVSDNTM VKLMTDGILL AEIQQDRLLM QYDTIIIDEA
     HERSLNIDFL LGYLKELLPR RPDLKIIITS ATIDPQRFSR HFNNAPIIEV SGRTYPVEVR
     YRPIVEEADD TERDQLQAIF DAVEELGQES PGDILIFMSG EREIRDTADA LNKLNLRHTE
     VLPLYARLSN SEQNRVFQSH SGRRIVLATN VAETSLTVPG IKYVIDPGTA RISRYSYRTK
     VQRLPIEPVS QASANQRKGR CGRVSEGICI RLYSEDDFLS RPEFTDPEIL RTNLASVILQ
     MTALGLGDIA AFPFVEAPDK RNIQDGVRLL EELGAITTDE QASAYKLTPL GRQLSQLPVD
     PRLARMVLEA QKHGCVREAM IVTSALSIQD PRERPMDKQQ ASDEKHRRFH DKESDFLAFV
     NLWNYLGEQQ KALSSNAFRR LCRTDYLNYL RVREWQDIYT QLRQVVKELG IPVNSEPAEY
     REIHIALLTG LLSHIGMKDA DKQEYTGARN ARFSIFPGSG LFKKPPKWTM VAELVETSRL
     WGRIAARIDP EWVEPVAQHL IKRSYSEPHW ERAQGAVMAT EKVTLYGLPI VAARKVNYSQ
     IDPALCRELF IRHALVEGDW QTRHAFFREN LKLRAEVEEL EHKSRRRDIL VDDETLFEFY
     DQRISHDVIS ARHFDSWWKK VSRETPDLLN FEKSMLIKEG AEKISKLDYP NFWHQGSLKL
     RLSYQFEPGA DADGVTVHIP LPLLNQVDES GFEWQIPGLR RELVIALIKS LPKPVRRNFV
     PAPNYAEAFL GRVTPLELTL LDALERELRR MTGVTVDRED WHLEQVPDHL KVTFRIVDEK
     NRKLQEGRSL TELKEALKGK VQETLSAVAD DGIEQSGLHI WSFGQLPESY EQKRGNYKVK
     AWPALVDERD SVAIKLFDNP LEQQQAMWSG LRRLLLLNIP SPIKYLHEKL PNKAKLGLYF
     NPYGKVLELI DDCISCGVDK LIDANGGPVW TEEGFAALHE KVRAELNDTV VDIAKQVEQI
     LTAVFNINKR LKGRVDMTMA LGLSDIKAQM GGLVYRGFVT GNGFKRLGDT LRYLQAIEKR
     LEKLAVDPHR DRAQMLKVES VQQAWQQWIN KLPPARREDE DVKEIRWMIE ELRVSYFAQQ
     LGTPYPISDK RILQAMEQIS S
//
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