ID A0A433JXV9_9GAMM Unreviewed; 303 AA.
AC A0A433JXV9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN Name=hflC {ECO:0000313|EMBL:RUR05603.1};
GN ORFNames=ELY15_14130 {ECO:0000313|EMBL:RUR05603.1};
OS Legionella sp. km772.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=2498111 {ECO:0000313|EMBL:RUR05603.1, ECO:0000313|Proteomes:UP000287796};
RN [1] {ECO:0000313|EMBL:RUR05603.1, ECO:0000313|Proteomes:UP000287796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=km772 {ECO:0000313|Proteomes:UP000287796};
RA Wu H.;
RT "Legionella sp,whole genome shotgun sequence.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: HflC and HflK could regulate a protease.
CC {ECO:0000256|PIRNR:PIRNR005651}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflC subfamily.
CC {ECO:0000256|ARBA:ARBA00007862, ECO:0000256|PIRNR:PIRNR005651}.
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:RUR05603.1}.
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DR EMBL; RZGQ01000223; RUR05603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433JXV9; -.
DR OrthoDB; 9812991at2; -.
DR Proteomes; UP000287796; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03405; SPFH_HflC; 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; IPR010200; HflC.
DR NCBIfam; TIGR01932; hflC; 2.
DR PANTHER; PTHR42911; MODULATOR OF FTSH PROTEASE HFLC; 1.
DR PANTHER; PTHR42911:SF1; MODULATOR OF FTSH PROTEASE HFLC; 1.
DR Pfam; PF01145; Band_7; 1.
DR PIRSF; PIRSF005651; HflC; 1.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RUR05603.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:RUR05603.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287796};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..190
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 303 AA; 33894 MW; 968CFE0F91E982E5 CRC64;
MSSVKAIISV LALFILIILF TCVFTVNEGQ QGILLRLGRL VNNAQGQVKV LNPGLHFKTP
FIENVRIFDT RIQTMDIKST RIVTKEKKDV MVDYYVKWQI TNLAQYFKST SGNQFKAETL
LEQQLNTLLR AQIGKRTISD VVSGGRDDVM TLLRDAAQKQ ANILGINVVD VRIKGIELPA
NTSNAIYQRM RADMQKIATR HRADGHAAAE QIQAKADADV TILLAKTRSK AQEIRAVGQA
EAAAIYTKAY SQNPSFFALY RSLLAYQGSF HSKKDILVLD QSSAFFDYFK QAMPKNDGVQ
SKK
//
