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Database: UniProt
Entry: A0A0R2JT69_9LACO
LinkDB: A0A0R2JT69_9LACO
Original site: A0A0R2JT69_9LACO 
ID   A0A0R2JT69_9LACO        Unreviewed;        81 AA.
AC   A0A0R2JT69;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=IV52_GL000435 {ECO:0000313|EMBL:KRN79030.1};
OS   Fructilactobacillus lindneri DSM 20690 = JCM 11027.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Fructilactobacillus.
OX   NCBI_TaxID=1122148 {ECO:0000313|EMBL:KRN79030.1, ECO:0000313|Proteomes:UP000051565};
RN   [1] {ECO:0000313|EMBL:KRN79030.1, ECO:0000313|Proteomes:UP000051565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20690 {ECO:0000313|EMBL:KRN79030.1,
RC   ECO:0000313|Proteomes:UP000051565};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRN79030.1}.
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DR   EMBL; JQBT01000032; KRN79030.1; -; Genomic_DNA.
DR   RefSeq; WP_054646201.1; NZ_MIYK01000001.1.
DR   AlphaFoldDB; A0A0R2JT69; -.
DR   STRING; 53444.AYR59_05620; -.
DR   GeneID; 61250315; -.
DR   PATRIC; fig|1122148.6.peg.454; -.
DR   OrthoDB; 9812389at2; -.
DR   Proteomes; UP000051565; 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; 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.
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:UP000051565};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00088}.
SQ   SEQUENCE   81 AA;  9329 MW;  DF516072A2D2FCEE CRC64;
     MINFDNLIKT IIKPLVKFPD DIKISHQDTD DFHEYILSTN EKDVGRVIGK RGRVAQTIRA
     IVYSVHVPDN KRIKLIINDG K
//
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