ID A0A0S8IP69_9BACT Unreviewed; 330 AA.
AC A0A0S8IP69;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=AMJ95_06725 {ECO:0000313|EMBL:KPK97882.1};
OS Omnitrophica WOR_2 bacterium SM23_72.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1703777 {ECO:0000313|EMBL:KPK97882.1, ECO:0000313|Proteomes:UP000051899};
RN [1] {ECO:0000313|EMBL:KPK97882.1, ECO:0000313|Proteomes:UP000051899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_72 {ECO:0000313|EMBL:KPK97882.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK97882.1}.
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DR EMBL; LJUU01000024; KPK97882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8IP69; -.
DR PATRIC; fig|1703777.3.peg.987; -.
DR Proteomes; UP000051899; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 42..222
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 330 AA; 37778 MW; 8A36F1FA9FEA0217 CRC64;
MNGQRVPTPN EIIDIGKKKF GDFSRMLPWI ILIFFLLIGL RGVIYSIGPD EVGVIQRFGK
YIALSSPGLH VKIPFGIDKV TPIKVEKIFK EEFGTRTSMS RTGTGYSSHY FDESLMLTGD
LNILDVRWIV QFKIKDPVKL LFAVRDPLDN IRDISEVVMR RFVGDYTVDS VLTTKREEID
DISQQEMQRI LDEYETGVHI VTVKLLDVNP PEKVKPAFNE VNEAKQEREK LINQAWEAYN
KVIPKARGTA EKTIREAEGY SLDKVNRARG ESKRFLATLT EYKKAPEVTQ ERLYLETLMN
ILPKAREKYI IDPKQSSILP LLKIGQKGGE
//
