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Database: UniProt
Entry: J2M3A4_9BURK
LinkDB: J2M3A4_9BURK
Original site: J2M3A4_9BURK 
ID   J2M3A4_9BURK            Unreviewed;       294 AA.
AC   J2M3A4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN   ORFNames=PMI16_01147 {ECO:0000313|EMBL:EJL92208.1};
OS   Herbaspirillum sp. CF444.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1144319 {ECO:0000313|EMBL:EJL92208.1, ECO:0000313|Proteomes:UP000007296};
RN   [1] {ECO:0000313|EMBL:EJL92208.1, ECO:0000313|Proteomes:UP000007296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF444 {ECO:0000313|EMBL:EJL92208.1,
RC   ECO:0000313|Proteomes:UP000007296};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(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:EJL92208.1}.
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DR   EMBL; AKJW01000021; EJL92208.1; -; Genomic_DNA.
DR   RefSeq; WP_007877290.1; NZ_AKJW01000021.1.
DR   AlphaFoldDB; J2M3A4; -.
DR   STRING; 1144319.PMI16_01147; -.
DR   MEROPS; I87.001; -.
DR   PATRIC; fig|1144319.3.peg.1159; -.
DR   eggNOG; COG0330; Bacteria.
DR   OrthoDB; 9812991at2; -.
DR   Proteomes; UP000007296; 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:EJL92208.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protease {ECO:0000313|EMBL:EJL92208.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          20..185
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
SQ   SEQUENCE   294 AA;  33512 MW;  8DB23BE3E0910456 CRC64;
     MSRLITSVIA VIVALWLLSS TIFVVEQRQS AIVFALGEVK QVVTEPGLHF KLPPPFQNVI
     YLDKRIQTLD TPDADRFITA EKKNVLVDSF VKWRIVDPRL YFISFGGDDR RAQDRLSQIV
     KAALNEEITK RTVREVISGE RGKVMDAIQR KVALEAKQIG AEIIDVRLRR VDYVDQINNS
     VYDRMKSERA RVANELRSTG AAESEKIRAD ADRQRVVILA EAYRDAEKIR GAGDAKASQI
     YAQAFGQNPE FYKFYRSLEA YRASFKNRHD LMVVDPNSEF FKYFKGVGGI STKK
//
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