ID I2BCV3_SHIBC Unreviewed; 968 AA.
AC I2BCV3; K6US38;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=RNA polymerase-associated protein RapA {ECO:0000256|HAMAP-Rule:MF_01821};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01821};
DE AltName: Full=ATP-dependent helicase HepA {ECO:0000256|HAMAP-Rule:MF_01821};
GN Name=hepA {ECO:0000313|EMBL:AFJ48357.1};
GN Synonyms=rapA {ECO:0000256|HAMAP-Rule:MF_01821};
GN OrderedLocusNames=EBL_c32940 {ECO:0000313|EMBL:AFJ48357.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ48357.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ48357.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(2012).
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 immobilized
CC on tightly supercoiled DNA. Does not activate transcription on linear
CC DNA. Probably not involved in DNA repair. {ECO:0000256|HAMAP-
CC Rule:MF_01821}.
CC -!- SUBUNIT: Interacts with the RNAP. Has a higher affinity for the core
CC RNAP than for the holoenzyme. Its ATPase activity is stimulated by
CC binding to RNAP. {ECO:0000256|HAMAP-Rule:MF_01821}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01821}.
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DR EMBL; CP001560; AFJ48357.1; -; Genomic_DNA.
DR RefSeq; WP_002464100.1; NZ_BAHA01000011.1.
DR AlphaFoldDB; I2BCV3; -.
DR STRING; 630626.EBL_c32940; -.
DR KEGG; ebt:EBL_c32940; -.
DR PATRIC; fig|630626.3.peg.3206; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000001955; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd18011; DEXDc_RapA; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.30.930; -; 1.
DR Gene3D; 3.30.360.80; -; 1.
DR Gene3D; 6.10.140.1500; -; 1.
DR Gene3D; 6.10.140.2230; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR HAMAP; MF_01821; Helicase_RapA; 1.
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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR040765; Tudor_1_RapA.
DR InterPro; IPR040766; Tudor_2_RapA.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12137; RapA_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 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; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_01821};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01821};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01821};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01821};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01821};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01821}; Reference proteome {ECO:0000313|Proteomes:UP000001955};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01821};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_01821}.
FT DOMAIN 164..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 490..643
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 280..283
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 968 AA; 109469 MW; D7A745C0841EAC44 CRC64;
MPFTLGQRWI SDTESELGLG TVVAMDARMV TLLFPATDEN RLYSRNDSPI TRVMFNPGDT
VTSHEGWQLK VDEVKAENGL LTYIGTRMDT EETGVPLREV FLDSKLVFSK PQDRLFAGQL
DRMDRFALRF RSRKYQSEQS RQPWSGLRGM RTSLIPHQLH IARDVGHRHA PRVLLADEVG
LGKTIEAGMI IHQQLLAGAA ERVLIIVPET LQHQWLVEML RRFNLRFALF DDERYAEAQH
DSTNPFDTEQ LIICSLDFVR RNKQRLENLC DAEWDMMVVD EAHHLVWSEE APSREYQAIE
QLAEHIPGVL LLTATPEQLG MESHFARLRL LDPNRFHDFG QFVAEQQHYR PVADAVALLL
EGNHLSRDEL NTLSELIGEQ DIEPLLQAAN SDSADAQDAR KELIHMLMDR HGTSRVLFRN
TRNGVKGFPQ RSLSTIKLPL PAQYQTAIKV SGIMGARKSA EERARDMLYP EQIYQEFEGD
SATWWNFDPR VEWLMGYLTR HRSQKVLVIC AKAATALQLE QVLREREGIR AAVFHEGMSI
IERDRAAAWF AEEDTGAQVL LCSEIGSEGR NFQFASNLVM FDLPFNPDLL EQRIGRLDRI
GQAHDIQIHV PYLEKTAQEV LVQWYHEGLD AFEHTCPTGR TIYDSVCSQL VEYLAAPDNT
TGFDELIKTC RAQHDALKVQ LEQGRDRLLE IHSNGGEAAQ QLADDIAAQD NDPALVNFAM
NLFDIIGINQ DDRGEHMIVL TPSDHMLVPD FPGLPEDGCT ITFNRDVALS REDAQLVTWE
HPIIRNGLDL ILSGDTGTSA ISLLKNKALP VGTLLVEMMY VVEAKAPKQL QLGRFLPATP
VRMLLDKNGT NLAAQVEFES FNRQLSAVNR HTGSKLVNAV QQDVHGILQL AETQVEKEAR
AIIDAARHEA DETLSAELAR LEALKAVNPN IRDDELEAIE SNRAQVMEAL DQASWRLDAL
RLIVVTHQ
//
