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Database: UniProt
Entry: A0A089IMS4_9BACL
LinkDB: A0A089IMS4_9BACL
Original site: A0A089IMS4_9BACL 
ID   A0A089IMS4_9BACL        Unreviewed;        76 AA.
AC   A0A089IMS4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=H70737_18980 {ECO:0000313|EMBL:AIQ24752.1};
OS   Paenibacillus sp. FSL H7-0737.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ24752.1, ECO:0000313|Proteomes:UP000029519};
RN   [1] {ECO:0000313|EMBL:AIQ24752.1, ECO:0000313|Proteomes:UP000029519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ24752.1,
RC   ECO:0000313|Proteomes:UP000029519};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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}.
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DR   EMBL; CP009279; AIQ24752.1; -; Genomic_DNA.
DR   RefSeq; WP_042128982.1; NZ_CP009279.1.
DR   AlphaFoldDB; A0A089IMS4; -.
DR   KEGG; paej:H70737_18980; -.
DR   eggNOG; COG1837; Bacteria.
DR   HOGENOM; CLU_132074_1_0_9; -.
DR   Proteomes; UP000029519; 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|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00088};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00088};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00088};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00088};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029519};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00088}.
SQ   SEQUENCE   76 AA;  8230 MW;  7ABE665F96574F82 CRC64;
     MEELVGVIAK ALVDHPEDVT VRAVEKDHLI VYELSVHPDD VGKVIGKQGR IAKALRTVVT
     SAAVKSDKRV TVDILS
//
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