ID   A0A1H2SDS2_9RHOB        Unreviewed;       399 AA.
AC   A0A1H2SDS2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN   ORFNames=SAMN05444336_101631 {ECO:0000313|EMBL:SDW29732.1};
OS   Albimonas donghaensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Albimonas.
OX   NCBI_TaxID=356660 {ECO:0000313|EMBL:SDW29732.1, ECO:0000313|Proteomes:UP000199118};
RN   [1] {ECO:0000313|EMBL:SDW29732.1, ECO:0000313|Proteomes:UP000199118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17890 {ECO:0000313|EMBL:SDW29732.1,
RC   ECO:0000313|Proteomes:UP000199118};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNMZ01000001; SDW29732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2SDS2; -.
DR   STRING; 356660.SAMN05444336_101631; -.
DR   OrthoDB; 9779595at2; -.
DR   Proteomes; UP000199118; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   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   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:SDW29732.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protease {ECO:0000313|EMBL:SDW29732.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199118}.
FT   DOMAIN          106..281
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          63..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   399 AA;  41719 MW;  3C1F48F25CB464E8 CRC64;
     MPFSNNSGGP WGGGGKDKNS GSGDRGPWGG GGRGGGGGGN GGGDQGPDMD ELLRQGRDRL
     KVIFGGGGQG GGGNRGGGGG SGLPEGIGRG GWIIAIIAAT GAWLAASLYT VDTSEQSVEL
     RLGEFAGIGN EGLNLAPWPL YTYEVLPVTR ENVINIGQNA VRSSGGSRQS DMGLMLTGDE
     NIVDVDYQVV WNIADPARFL FNLAEPEATI RAVSEAAMRE VIGKSELAPI LNRDRAIVSQ
     DVQALIQSTL EGYEAGVNIV RVNFDKADPP REVIDAFRDV QAAGQDRVRS ENTAEAYANR
     ALAEARGQSA QLVQEAEAYN AQTVNDAQGD AARFLAILAE YRNAEDVTRK RLYLETMEKV
     LGDVDKIVIE DGVSGSGSGG GGGVLPYLPL DQLRKGGNQ
//