ID A0A1M5SU50_9CLOT Unreviewed; 75 AA.
AC A0A1M5SU50;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN02745196_00315 {ECO:0000313|EMBL:SHH42055.1};
OS Clostridium collagenovorans DSM 3089.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121306 {ECO:0000313|EMBL:SHH42055.1, ECO:0000313|Proteomes:UP000184526};
RN [1] {ECO:0000313|EMBL:SHH42055.1, ECO:0000313|Proteomes:UP000184526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3089 {ECO:0000313|EMBL:SHH42055.1,
RC ECO:0000313|Proteomes:UP000184526};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQXP01000003; SHH42055.1; -; Genomic_DNA.
DR RefSeq; WP_072829386.1; NZ_FQXP01000003.1.
DR AlphaFoldDB; A0A1M5SU50; -.
DR STRING; 1121306.SAMN02745196_00315; -.
DR OrthoDB; 9812389at2; -.
DR Proteomes; UP000184526; 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 Reference proteome {ECO:0000313|Proteomes:UP000184526};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00088, ECO:0000256|PROSITE-
KW ProRule:PRU00117}.
SQ SEQUENCE 75 AA; 8278 MW; 6BD8EE9D4EA78A4F CRC64;
MKEVLEVIAK SLVDNPEMVD VKEVVGEHSI ILELKVSQED MGKIIGKQGR IAKAIRTVVK
AAAIKENKRV VVEII
//