ID A0A0M0HKE6_VIBNE Unreviewed; 169 AA.
AC A0A0M0HKE6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chaperone protein skp {ECO:0000256|PIRNR:PIRNR002094};
GN ORFNames=AKJ17_15785 {ECO:0000313|EMBL:KOO02530.1};
OS Vibrio nereis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=693 {ECO:0000313|EMBL:KOO02530.1, ECO:0000313|Proteomes:UP000037515};
RN [1] {ECO:0000313|Proteomes:UP000037515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19584 {ECO:0000313|Proteomes:UP000037515};
RA Giubergia S., Machado H., Mateiu R.V., Gram L.;
RT "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family
RT isolated from the Solomon Islands.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular chaperone that interacts specifically with outer
CC membrane proteins, thus maintaining the solubility of early folding
CC intermediates during passage through the periplasm.
CC {ECO:0000256|PIRNR:PIRNR002094}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|PIRNR:PIRNR002094}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|PIRNR:PIRNR002094}.
CC -!- SIMILARITY: Belongs to the skp family. {ECO:0000256|PIRNR:PIRNR002094}.
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:KOO02530.1}.
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DR EMBL; LHPJ01000016; KOO02530.1; -; Genomic_DNA.
DR RefSeq; WP_053396772.1; NZ_LHPJ01000016.1.
DR AlphaFoldDB; A0A0M0HKE6; -.
DR STRING; 693.AKJ17_15785; -.
DR PATRIC; fig|693.5.peg.3218; -.
DR OrthoDB; 5624238at2; -.
DR Proteomes; UP000037515; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 3.30.910.20; Skp domain; 1.
DR InterPro; IPR005632; Chaperone_Skp.
DR InterPro; IPR024930; Skp_dom_sf.
DR PANTHER; PTHR35089; CHAPERONE PROTEIN SKP; 1.
DR PANTHER; PTHR35089:SF1; CHAPERONE PROTEIN SKP; 1.
DR Pfam; PF03938; OmpH; 1.
DR PIRSF; PIRSF002094; OMP26_Skp; 1.
DR SMART; SM00935; OmpH; 1.
DR SUPFAM; SSF111384; OmpH-like; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|PIRNR:PIRNR002094};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Periplasm {ECO:0000256|PIRNR:PIRNR002094};
KW Reference proteome {ECO:0000313|Proteomes:UP000037515};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..169
FT /note="Chaperone protein skp"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005600039"
FT COILED 49..123
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 169 AA; 19093 MW; B4796245ACDC15A6 CRC64;
MNKTIKAAGL GLLIMTSSLF ANAAEAAQKV GYINTAQVFQ ALPQREVVSQ KMQKEFKDKV
DELKSIQAQA KTKIEKLKRD GELMSEGDVE KLRIEIAQLD SKYKVKAQAL EQATARREAQ
EKQKLFKVIQ DAVKKVAEKE GYDMIVDIQA MQYGKPEYNI SEKVIKQIK
//
