ID F5Z513_ALTNA Unreviewed; 942 AA.
AC F5Z513;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=rapA {ECO:0000256|HAMAP-Rule:MF_01821};
GN OrderedLocusNames=ambt_15350 {ECO:0000313|EMBL:AEF04580.1};
OS Alteromonas naphthalenivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF04580.1, ECO:0000313|Proteomes:UP000000683};
RN [1] {ECO:0000313|EMBL:AEF04580.1, ECO:0000313|Proteomes:UP000000683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC {ECO:0000313|Proteomes:UP000000683};
RX PubMed=21705606; DOI=10.1128/JB.05252-11;
RA Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA Oh T.K., Kim J.F.;
RT "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT bacterium Alteromonas sp. strain SN2.";
RL J. Bacteriol. 193:4292-4293(2011).
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; CP002339; AEF04580.1; -; Genomic_DNA.
DR RefSeq; WP_013785504.1; NC_015554.1.
DR AlphaFoldDB; F5Z513; -.
DR KEGG; alt:ambt_15350; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000000683; 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};
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 167..338
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 475..622
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 284..287
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 180..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 942 AA; 106130 MW; AEC98915A6F26322 CRC64;
MSSGNPFSIG QRWLSNSETE LGLGAVISVD FRSVELFFPA TGEARMYTKQ DAPLTRLVFD
IGETVKSQDG WQMTISEIEE SQGVCIYFGI REDTKAQVRL SETLLDHHIR LNQPERRLFS
EQLDHPKWFD LRLNALNHQY DYLRSSTLGL AGARISLIPH QLHIASEVGS RHAPRVLLAD
EVGLGKTIEA ALIIHQQLRT GRAQRVLILV PDSLVHQWLV EMLRRINLPF AIFDESRCEA
LDDDGETNPF DNDQLVLCSI DFLSQSEKRQ QQIQAASWDL MVVDEAHHLA WSADAPSAEY
TLVEALANET PGVLLLTATP DQLGHESHFA RLRLLDPARF HSYEAFLTEE SRYSQLADAV
APLLSDTTPD EKQRTKLTDF APDVMENAGN LAQPEARREL VHQLIDCHGT GRMLFRNRRA
NIEGFPDRVL LGYQLELPEV YESAVTGGDL THALYPERMP SVVNSWMDED PRVGWLLDFM
QSVKPEKILL ICASARTAQE LGEVIRTQTG VRHSVFHEGM TIVERDKAAH YFSDEEDGAQ
ILLCSEIGSE GRNFQFAHHL VLFDLPVTPD LLEQRIGRLD RIGQTQTVEI HVPYLKNTAQ
HVLVDWYHEG LNAFEKTCPT GSGVFDDVKT LLIGACLHPH DLHTRDELIN LSTTLNSQLV
AQLEAGRDRL LELNASGEGR VEQLLEDIIL LDNSQDLSRF MGRLFDAIGV QQEEKGSDCF
ILMPTESMVS QLPGLDPEGM TVTYKRRVAT TLENVQFLSW DHPLVHTAID LVLSDVHGKS
SIGFIADPDL PKGAYWLEAL FVLDANAPKA LQLGRFLPQT PLRICLDAQG NQVDLTFEIK
RKVNRKISHQ LIKALQQPLT LAIESSRKLA HQQANQKLHD ALQDMHKTLN SEIQRLVDLQ
KRNPSVRDSE IEFIENQMNA LDKVIQGADV QFDALRLVVN NP
//
