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Database: UniProt
Entry: K1MNM3_9LACT
LinkDB: K1MNM3_9LACT
Original site: K1MNM3_9LACT 
ID   K1MNM3_9LACT            Unreviewed;        88 AA.
AC   K1MNM3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=HMPREF9707_00497 {ECO:0000313|EMBL:EKB57759.1};
OS   Falseniella ignava CCUG 37419.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Falseniella.
OX   NCBI_TaxID=883112 {ECO:0000313|EMBL:EKB57759.1, ECO:0000313|Proteomes:UP000005147};
RN   [1] {ECO:0000313|EMBL:EKB57759.1, ECO:0000313|Proteomes:UP000005147}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 37419 {ECO:0000313|EMBL:EKB57759.1,
RC   ECO:0000313|Proteomes:UP000005147};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Facklamia ignava CCUG 37419.";
RL   Submitted (JUL-2012) 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:EKB57759.1}.
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DR   EMBL; AGZE01000013; EKB57759.1; -; Genomic_DNA.
DR   RefSeq; WP_006701161.1; NZ_JH932300.1.
DR   AlphaFoldDB; K1MNM3; -.
DR   STRING; 883112.HMPREF9707_00497; -.
DR   PATRIC; fig|883112.3.peg.493; -.
DR   eggNOG; COG1837; Bacteria.
DR   HOGENOM; CLU_132074_1_0_9; -.
DR   Proteomes; UP000005147; 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:UP000005147};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00088}.
SQ   SEQUENCE   88 AA;  10337 MW;  2CFCA156546895E1 CRC64;
     MLDIKALIQT MIEPLIEFPE DFEIKVVEGE EFTEYHLHLN PEDIGRVIGR RGRVIRSIRT
     IVYSIRQRGQ KRSKIVVQDD ATDQLEDE
//
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