ID J4XS72_9FIRM Unreviewed; 75 AA.
AC J4XS72;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=HMPREF1148_1118 {ECO:0000313|EMBL:EJO23131.1};
OS Selenomonas sp. FOBRC6.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=936572 {ECO:0000313|EMBL:EJO23131.1, ECO:0000313|Proteomes:UP000006984};
RN [1] {ECO:0000313|EMBL:EJO23131.1, ECO:0000313|Proteomes:UP000006984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOBRC6 {ECO:0000313|EMBL:EJO23131.1,
RC ECO:0000313|Proteomes:UP000006984};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
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:EJO23131.1}.
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DR EMBL; ALKG01000053; EJO23131.1; -; Genomic_DNA.
DR RefSeq; WP_006306836.1; NZ_ALKG01000053.1.
DR AlphaFoldDB; J4XS72; -.
DR STRING; 936572.HMPREF1148_1118; -.
DR GeneID; 84787281; -.
DR PATRIC; fig|936572.3.peg.688; -.
DR eggNOG; COG1837; Bacteria.
DR Proteomes; UP000006984; 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.
DR PROSITE; PS50084; KH_TYPE_1; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00117}.
SQ SEQUENCE 75 AA; 8224 MW; 1AB6C13159C0DDEF CRC64;
MKEIVEVIAK SLVDHPEAVV VDETQDDQEI ILRLRVAEDD MGKVIGKQGR IAKALRSVVK
AAATKENKRA TVEIG
//
