ID D8MVU6_ERWBE Unreviewed; 443 AA.
AC D8MVU6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=ATP-dependent RNA helicase SrmB {ECO:0000256|HAMAP-Rule:MF_00967};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00967};
GN Name=srmB {ECO:0000256|HAMAP-Rule:MF_00967};
GN OrderedLocusNames=EbC_34220 {ECO:0000313|EMBL:CAX60953.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX60953.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX60953.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- FUNCTION: DEAD-box RNA helicase involved in the assembly of the 50S
CC ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP
CC hydrolysis and RNA unwinding activity. {ECO:0000256|HAMAP-
CC Rule:MF_00967}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00967};
CC -!- SUBUNIT: Interacts with the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00967}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00967}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. SrmB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00967}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FP236843; CAX60953.1; -; Genomic_DNA.
DR RefSeq; WP_013203438.1; NC_014306.1.
DR AlphaFoldDB; D8MVU6; -.
DR STRING; 634500.EbC_34220; -.
DR KEGG; ebi:EbC_34220; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_28_3_6; -.
DR Proteomes; UP000008793; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00967; DEAD_helicase_SrmB; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR028621; DEAD_helicase_SrmB.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF3; ATP-DEPENDENT RNA HELICASE SRMB; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00967}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00967};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00967};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00967};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00967}; Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00967}.
FT DOMAIN 4..32
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 35..209
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 238..387
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 377..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..32
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 377..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 50000 MW; F35F1A00354DF7C1 CRC64;
MTVTTFSELE LDESLLKALQ EKGYTRPTAI QAAAIPPALE GRDVLGSAPT GTGKTAAYLL
PVLQHLLDFP RKKSGPPRVL ILTPTRELAM QVADQARELA KYTHLDIATI TGGVAYMNHA
EVFSENQDVV VATTGRLLQY IKEENFDCRA VESLILDEAD RMLDMGFAQD IETIAAETRW
RKQTLLFSAT LEGDAIKDFS ERLLNEPEEI EADPARRERK KILQWYYRAD DVKHKTALLI
HMLKQPEVTR SVVFVRKRER VHELCGWLRE AGINTSYLEG ELEQFKRNEA IKRVVDGRVN
VLVATDVAAR GIDIEDVSHV FNFDMPRTSD TYLHRIGRTG RAGKKGIAIS LVEAHDNVLL
GKVTRYIKEP LKSRTIDELR PTTRPPSEKL NGKPSKKVLA KRKELKQTEA KEAQPRAKER
HRDTKNIGKR RKPTAVAKPD SAE
//
