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Database: UniProt
Entry: I4VPB8_9GAMM
LinkDB: I4VPB8_9GAMM
Original site: I4VPB8_9GAMM 
ID   I4VPB8_9GAMM            Unreviewed;       289 AA.
AC   I4VPB8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN   ORFNames=UU9_10452 {ECO:0000313|EMBL:EIL89059.1};
OS   Rhodanobacter fulvus Jip2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL89059.1, ECO:0000313|Proteomes:UP000004210};
RN   [1] {ECO:0000313|EMBL:EIL89059.1, ECO:0000313|Proteomes:UP000004210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX   PubMed=22843592; DOI=10.1128/JB.00871-12;
RA   Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA   Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA   Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT   "Genome sequences for six rhodanobacter strains, isolated from soils and
RT   the terrestrial subsurface, with variable denitrification capabilities.";
RL   J. Bacteriol. 194:4461-4462(2012).
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:EIL89059.1}.
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DR   EMBL; AJXU01000042; EIL89059.1; -; Genomic_DNA.
DR   RefSeq; WP_007081727.1; NZ_AJXU01000042.1.
DR   AlphaFoldDB; I4VPB8; -.
DR   STRING; 1163408.UU9_10452; -.
DR   MEROPS; I87.001; -.
DR   PATRIC; fig|1163408.3.peg.2143; -.
DR   eggNOG; COG0330; Bacteria.
DR   OrthoDB; 9812991at2; -.
DR   Proteomes; UP000004210; 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   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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004210};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          19..183
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
SQ   SEQUENCE   289 AA;  32780 MW;  99E710BF78E6356D CRC64;
     MSRIAAGVVA VLLILLGLNS MFVVREGHSA LLLQFGRIVH TDYQPGLHFK IPVIQQVMHF
     DKRILSLDAP PERYFTSEKK SVNVDFYVKW RVLDNAAYYR ATGGDQLQAA QRLTPIVKDA
     LRFEFNARTL PDLISGGRKD ITERVRAQTD ASARKNLGIA VVDVRIKRID LPNEVSESVY
     KRMRAERLQL ANELRYTGQE AAEKIQADAD RQGQVLRADA MRDAAKIRGE GDAQAAAIYA
     KAYGQDAEFF TFYRSLAAYR KSFEDGKGML ILKPDSEFMR YFNQPVQKR
//
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