ID A0A1Y3NYV0_9PSED Unreviewed; 390 AA.
AC A0A1Y3NYV0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=AUC60_16755 {ECO:0000313|EMBL:OUM72748.1};
OS Pseudomonas caspiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1451454 {ECO:0000313|EMBL:OUM72748.1, ECO:0000313|Proteomes:UP000195440};
RN [1] {ECO:0000313|EMBL:OUM72748.1, ECO:0000313|Proteomes:UP000195440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBF102 {ECO:0000313|EMBL:OUM72748.1,
RC ECO:0000313|Proteomes:UP000195440};
RX PubMed=28552245; DOI=10.1016/j.syapm.2017.04.002;
RA Busquets A., Gomila M., Beiki F., Mulet M., Rahimian H., Garcia-Valdes E.,
RA Lalucat J.;
RT "Pseudomonas caspiana sp. nov., a citrus pathogen in the Pseudomonas
RT syringae phylogenetic group.";
RL Syst. Appl. Microbiol. 40:266-273(2017).
CC -!- FUNCTION: HflC and HflK could encode or regulate a protease.
CC {ECO:0000256|RuleBase:RU364113}.
CC -!- SUBUNIT: HflC and HflK may interact to form a multimeric complex.
CC {ECO:0000256|RuleBase:RU364113}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU364113}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflK subfamily.
CC {ECO:0000256|ARBA:ARBA00006971, ECO:0000256|RuleBase:RU364113}.
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:OUM72748.1}.
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DR EMBL; LOHF01000014; OUM72748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3NYV0; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000195440; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd03404; SPFH_HflK; 1.
DR Gene3D; 3.30.479.30; Band 7 domain; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR010201; HflK.
DR InterPro; IPR020980; Membrane_HflK_N.
DR InterPro; IPR001972; Stomatin_HflK_fam.
DR NCBIfam; TIGR01933; hflK; 1.
DR PANTHER; PTHR43327:SF2; MODULATOR OF FTSH PROTEASE HFLK; 1.
DR PANTHER; PTHR43327; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF12221; HflK_N; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 86..246
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 43014 MW; 741CB1C4C64C4739 CRC64;
MAWNEPGGNS NNQDPWGGKR KGDDRKGPPD LDEAFRKLQE SLNGLFGGGK KRSGGDGGGN
GNPGKGGGFG LLGIGLVVLV AIWLYSAIYV VDEQEQAVVL RFGQYHETVG SGLNIYFPPF
DRKYMENVTR ERAYSKQGQM LTEDENIVEV PLTVQYKISN LRDFVLNVDQ PEVSLQHATE
SALRHVVGST AMDQVLTEGR ELMASEIKER LQRFLDTYRT GITVTQVNVQ SAAAPREVQE
AFDDVIRARE DEQRSRNQAE TYANGVIPEA RGQAQRIIED ANGYRDEVIS RAKGEADRFT
KLVAEYRKAP EVTRERLYLD TMQELFTNTS KVLVTGEKGG NNLLYLPLDK MIENGRSGNS
AAPTNGAAAV GADAGARAAE IQQPRTRETR
//
