ID S1R278_9ENTE Unreviewed; 82 AA.
AC S1R278;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=OMO_00965 {ECO:0000313|EMBL:ESK61977.1};
OS Enterococcus cecorum DSM 20682 = ATCC 43198.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1121864 {ECO:0000313|EMBL:ESK61977.1, ECO:0000313|Proteomes:UP000017415};
RN [1] {ECO:0000313|EMBL:ESK61977.1, ECO:0000313|Proteomes:UP000017415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43198 {ECO:0000313|EMBL:ESK61977.1,
RC ECO:0000313|Proteomes:UP000017415};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus cecorum DSM 20682 (= ATCC 43198)
RT (Illumina assembly).";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK61977.1}.
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DR EMBL; AHYS01000004; ESK61977.1; -; Genomic_DNA.
DR RefSeq; WP_016251268.1; NZ_KI535313.1.
DR AlphaFoldDB; S1R278; -.
DR STRING; 44008.GCA_001318175_02273; -.
DR GeneID; 60872115; -.
DR PATRIC; fig|1121864.4.peg.1083; -.
DR eggNOG; COG1837; Bacteria.
DR HOGENOM; CLU_132074_1_2_9; -.
DR OrthoDB; 9812389at2; -.
DR Proteomes; UP000017415; Unassembled WGS sequence.
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|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW 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 Reference proteome {ECO:0000313|Proteomes:UP000017415};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00088}.
SQ SEQUENCE 82 AA; 9201 MW; DBB7B0E9E60B4C0F CRC64;
MKDLQALVLT IVRPLVTQPD QVQLEVSESE EFIEYNLTVA PEDIGRIIGK QGRVAKAIRT
IVYSVRVNGP KKVRLNILDG KE
//
