ID A0A2A2GBV8_9BACT Unreviewed; 339 AA.
AC A0A2A2GBV8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN Name=hflK {ECO:0000313|EMBL:PAU94353.1};
GN ORFNames=CK503_05990 {ECO:0000313|EMBL:PAU94353.1};
OS Aliifodinibius salipaludis.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX NCBI_TaxID=2032627 {ECO:0000313|EMBL:PAU94353.1, ECO:0000313|Proteomes:UP000218831};
RN [1] {ECO:0000313|EMBL:PAU94353.1, ECO:0000313|Proteomes:UP000218831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN023 {ECO:0000313|EMBL:PAU94353.1,
RC ECO:0000313|Proteomes:UP000218831};
RA Liu D., Zhang G.;
RT "Aliifodinibius alkalisoli sp. nov., isolated from saline alkaline soil.";
RL Submitted (AUG-2017) 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 -!- 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:PAU94353.1}.
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DR EMBL; NSKE01000004; PAU94353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2GBV8; -.
DR OrthoDB; 9809197at2; -.
DR Proteomes; UP000218831; 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:PAU94353.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Protease {ECO:0000313|EMBL:PAU94353.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218831};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 38..218
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 339 AA; 38495 MW; 7E5FE8CF9CADAD21 CRC64;
MAQDNNFSGM DIPPQLKKLG SNIRYIILGA LVVVIAFSSF FTVNPEEVGI VTRFGEFTRT
AYPGLNFKAP FVEEVRYVPI ERQLKHEFGY RTTSSGVRSS YQKEGYKDES LMLTGDLNLA
DVEWVVQYRV DDPYDFLFKI RNPEQTLRDI SESAMRQIVG DRTVNEVLTV GRAEVAMKAQ
DLIQKICNEY ESGIRIEQIV LQDINPPDPV KPSFNAVNEA QQQKETLINE AKSEYNKVIP
RAKGRAQETI QRAEGYAVNR VNRAQGEASR FNQLYQEYVK APEVTKRRLY LETLEEILPK
LGNKIVTDQN GNSVLPLLQM QMDGVNVNKS NANSKNQGN
//
