ID M1LMI1_9PROT Unreviewed; 290 AA.
AC M1LMI1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN ORFNames=CDSE_0646 {ECO:0000313|EMBL:AGF46937.1};
OS Candidatus Kinetoplastibacterium desouzaii TCC079E.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208919 {ECO:0000313|EMBL:AGF46937.1, ECO:0000313|Proteomes:UP000011547};
RN [1] {ECO:0000313|EMBL:AGF46937.1, ECO:0000313|Proteomes:UP000011547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC079E {ECO:0000313|EMBL:AGF46937.1,
RC ECO:0000313|Proteomes:UP000011547};
RX PubMed=23345457;
RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA Teixeira M.M., Camargo E.P., Buck G.A.;
RT "Genome evolution and phylogenomic analysis of candidatus
RT kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT and angomonas.";
RL Genome Biol. Evol. 5:338-350(2013).
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}.
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DR EMBL; CP003803; AGF46937.1; -; Genomic_DNA.
DR RefSeq; WP_015396348.1; NC_020294.1.
DR AlphaFoldDB; M1LMI1; -.
DR STRING; 1208919.CDSE_0646; -.
DR KEGG; kde:CDSE_0646; -.
DR PATRIC; fig|1208919.3.peg.375; -.
DR eggNOG; COG0330; Bacteria.
DR HOGENOM; CLU_059167_3_0_4; -.
DR OrthoDB; 9812991at2; -.
DR Proteomes; UP000011547; Chromosome.
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:AGF46937.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:AGF46937.1};
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 290 AA; 32979 MW; 3B6CD4700559172D CRC64;
MQRVFSILCG FLIICFFASS TLFVINERSH ALVFSLGEIS REISTPGLYF KLPAPFQNVE
FLDKRILTIE SKDAERIQTS EKKNLSIDSF VKWRIANPKL FYITFGGNER AAKERLQAQI
RDALNASVNI RTVKEVVSVE RGKIMTEILN NVASRAKPLG VEIVDVRLRR IEFAPEISKS
VYRRMEAERT RVANELRSIG AAESEKIRAE ADRSREEILA KANTRAQIIM GEGDAEASAI
YASSFGKNHN FYKFYKSLEA YKKSFATKND TLIVDPTSDF FQFMKCSNVK
//
