ID M5PQF9_DESAF Unreviewed; 77 AA.
AC M5PQF9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=PCS_02807 {ECO:0000313|EMBL:EMG36304.1};
OS Desulfocurvibacter africanus PCS.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=1262666 {ECO:0000313|EMBL:EMG36304.1, ECO:0000313|Proteomes:UP000011922};
RN [1] {ECO:0000313|EMBL:EMG36304.1, ECO:0000313|Proteomes:UP000011922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCS {ECO:0000313|EMBL:EMG36304.1,
RC ECO:0000313|Proteomes:UP000011922};
RX PubMed=23580709;
RA Brown S.D., Utturkar S.M., Arkin A.P., Deutschbauer A.M., Elias D.A.,
RA Hazen T.C., Chakraborty R.;
RT "Draft Genome Sequence for Desulfovibrio africanus Strain PCS.";
RL Genome Announc. 1:E00144-13(2013).
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:EMG36304.1}.
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DR EMBL; AOSV01000030; EMG36304.1; -; Genomic_DNA.
DR RefSeq; WP_005988212.1; NZ_AOSV01000030.1.
DR AlphaFoldDB; M5PQF9; -.
DR PATRIC; fig|1262666.3.peg.2840; -.
DR OrthoDB; 9812389at2; -.
DR Proteomes; UP000011922; 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 77 AA; 8347 MW; 3D8E49F54110DB44 CRC64;
MPKELITYLV KALVDHPEMV QVTEVVGENV IILEVKVAKE DVGKVIGKSG RTVLALRDIL
AAVAGKGKQR VVLDILE
//
