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Database: UniProt
Entry: A0A177MWJ9_9GAMM
LinkDB: A0A177MWJ9_9GAMM
Original site: A0A177MWJ9_9GAMM 
ID   A0A177MWJ9_9GAMM        Unreviewed;       320 AA.
AC   A0A177MWJ9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN   ORFNames=A1359_01950 {ECO:0000313|EMBL:OAI10076.1};
OS   Methylomonas lenta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=980561 {ECO:0000313|EMBL:OAI10076.1, ECO:0000313|Proteomes:UP000078476};
RN   [1] {ECO:0000313|EMBL:OAI10076.1, ECO:0000313|Proteomes:UP000078476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-45370 {ECO:0000313|EMBL:OAI10076.1,
RC   ECO:0000313|Proteomes:UP000078476};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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:OAI10076.1}.
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DR   EMBL; LUUI01000160; OAI10076.1; -; Genomic_DNA.
DR   RefSeq; WP_066987647.1; NZ_LUUI01000160.1.
DR   AlphaFoldDB; A0A177MWJ9; -.
DR   STRING; 980561.A1359_01950; -.
DR   OrthoDB; 9812991at2; -.
DR   Proteomes; UP000078476; 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; 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   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:OAI10076.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protease {ECO:0000313|EMBL:OAI10076.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078476};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..320
FT                   /note="Protein HflC"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008068502"
FT   DOMAIN          20..212
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
SQ   SEQUENCE   320 AA;  36631 MW;  2A56ED5E4662A1C5 CRC64;
     MKLSIKAGLL LGTVATVLML SAYTVNQAEQ VIITQFGRPI GDPVTTPGLH FKMPFVQQVN
     SFDKRYLAWD GPMVEMSTKD KTYVQVDTFA RWRITDPMRY YLRLRDERSA QSRLEDILGS
     ETRTAIARHE LIEVVRTDKD RKPFVDETLG DLAGEGTLGV LRPIRVGRVA IEKHVFDAAA
     PKLEEFGIEL LDVRFKRINY NQQVLERIYQ RMISERLQIA QRFRSEGEGE AARIKGNKER
     DLNEIESTAY KQVQEIQGQA DAKATEIYAK AYAQNPEAIK FYKFVKTMET YRKVINNDAS
     IVLSTNSELF GLLKRVQKGE
//
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