ID E6UEM0_RUMA7 Unreviewed; 77 AA.
AC E6UEM0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=RNA-binding protein KhpA {ECO:0000256|HAMAP-Rule:MF_00088};
DE AltName: Full=KH-domain protein A {ECO:0000256|HAMAP-Rule:MF_00088};
GN Name=khpA {ECO:0000256|HAMAP-Rule:MF_00088};
GN OrderedLocusNames=Rumal_0420 {ECO:0000313|EMBL:ADU20975.1};
OS Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 /
OS 7).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=697329 {ECO:0000313|EMBL:ADU20975.1, ECO:0000313|Proteomes:UP000006919};
RN [1] {ECO:0000313|EMBL:ADU20975.1, ECO:0000313|Proteomes:UP000006919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7
RC {ECO:0000313|Proteomes:UP000006919};
RX PubMed=21914885; DOI=10.1128/JB.05621-11;
RA Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., Cheng J.F.,
RA Detter C., Detter J.C., Goodwin L.A., Han C.S., Hauser L.J., Ivanova N.N.,
RA Kyrpides N.C., Land M.L., Lapidus A., Lucas S., Ovchinnikova G.,
RA Pitluck S., Tapia R., Woyke T., Boyum J., Mead D., Weimer P.J.;
RT "Complete genome of the cellulolytic ruminal bacterium Ruminococcus albus
RT 7.";
RL J. Bacteriol. 193:5574-5575(2011).
CC -!- FUNCTION: A probable RNA chaperone. Forms a complex with KhpB which
CC binds to cellular RNA and controls its expression. Plays a role in
CC peptidoglycan (PG) homeostasis and cell length regulation.
CC {ECO:0000256|HAMAP-Rule:MF_00088}.
CC -!- SUBUNIT: Forms a complex with KhpB. {ECO:0000256|HAMAP-Rule:MF_00088}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00088}.
CC -!- SIMILARITY: Belongs to the KhpA RNA-binding protein family.
CC {ECO:0000256|HAMAP-Rule:MF_00088}.
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DR EMBL; CP002403; ADU20975.1; -; Genomic_DNA.
DR RefSeq; WP_013497167.1; NZ_JHYT01000030.1.
DR AlphaFoldDB; E6UEM0; -.
DR STRING; 697329.Rumal_0420; -.
DR KEGG; ral:Rumal_0420; -.
DR eggNOG; COG1837; Bacteria.
DR HOGENOM; CLU_132074_1_1_9; -.
DR OrthoDB; 9812389at2; -.
DR Proteomes; UP000006919; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd22533; KH-II_YlqC-like; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR HAMAP; MF_00088; KhpA; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR020627; KhpA.
DR PANTHER; PTHR34654:SF1; RNA-BINDING PROTEIN KHPA; 1.
DR PANTHER; PTHR34654; UPF0109 PROTEIN SCO5592; 1.
DR Pfam; PF13083; KhpA-B_KH; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00088};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00088};
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00088};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00088};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00088}.
SQ SEQUENCE 77 AA; 8487 MW; 243B6B81CD309720 CRC64;
MEELLKTIVT DLVEDKTAVE VSVDEPNDEG VIVYHLHVAQ DDMGRVIGKQ GRIAKAIRVV
MRAAASKLGQ KIMVEID
//
