ID W9HC41_9PROT Unreviewed; 343 AA.
AC W9HC41;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN ORFNames=N825_28535 {ECO:0000313|EMBL:EWY41453.1};
OS Skermanella stibiiresistens SB22.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Skermanella.
OX NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY41453.1, ECO:0000313|Proteomes:UP000019486};
RN [1] {ECO:0000313|EMBL:EWY41453.1, ECO:0000313|Proteomes:UP000019486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB22 {ECO:0000313|EMBL:EWY41453.1,
RC ECO:0000313|Proteomes:UP000019486};
RA Zhu W., Wang G.;
RT "The genome sequence of Skermanella stibiiresistens.";
RL Submitted (AUG-2013) 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:EWY41453.1}.
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; AVFL01000004; EWY41453.1; -; Genomic_DNA.
DR RefSeq; WP_037449359.1; NZ_AVFL01000004.1.
DR AlphaFoldDB; W9HC41; -.
DR STRING; 1385369.N825_28535; -.
DR PATRIC; fig|1385369.3.peg.1649; -.
DR OrthoDB; 9812991at2; -.
DR Proteomes; UP000019486; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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 InterPro; IPR001972; Stomatin_HflK_fam.
DR NCBIfam; TIGR01932; hflC; 1.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019486};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 21..183
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 299..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 37227 MW; B68014DE55152002 CRC64;
MNKKLAIIGI VVVVLGILAS ASLFTVNETQ QALVLQFGEP RRVIQEPGLK AKIPFIQNVV
LYDRRVLDVD PPVEQVILAD QKRLDVDAFA RYRITDPLRF FQSVGSELVL EQRLSTVVVS
ALRRVLGNVT VLSILSDERP RVMADIRTQV NGEAQRFGIE VVDVRIRRAD LPEETSQSIF
ARMRSERERE AAEFRAQGQE QAQQIRSRAE RERTVIIAEA QRDSQVLRGE GDNQAFRIIA
EATGRDAEFY SFYRTLQAYR DSLRNEDTTM VLSPTGDFFK YFGNLGGVPS GAVANGSGAG
GSGAGGGNGG NGGPAGASNQ GPAAIPSAPA TQGAENTQPA PAN
//
