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Database: UniProt
Entry: B9KGT2_ANAMF
LinkDB: B9KGT2_ANAMF
Original site: B9KGT2_ANAMF 
ID   B9KGT2_ANAMF            Unreviewed;       318 AA.
AC   B9KGT2;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN   Name=hflC {ECO:0000313|EMBL:ACM49636.1};
GN   OrderedLocusNames=AMF_804 {ECO:0000313|EMBL:ACM49636.1};
OS   Anaplasma marginale (strain Florida).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=320483 {ECO:0000313|EMBL:ACM49636.1, ECO:0000313|Proteomes:UP000007307};
RN   [1] {ECO:0000313|EMBL:ACM49636.1, ECO:0000313|Proteomes:UP000007307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Florida {ECO:0000313|EMBL:ACM49636.1,
RC   ECO:0000313|Proteomes:UP000007307};
RX   PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA   Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA   Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT   "Conservation in the face of diversity: multistrain analysis of an
RT   intracellular bacterium.";
RL   BMC Genomics 10:16-16(2009).
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; CP001079; ACM49636.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9KGT2; -.
DR   STRING; 320483.AMF_804; -.
DR   MEROPS; I87.001; -.
DR   KEGG; amf:AMF_804; -.
DR   eggNOG; COG0330; Bacteria.
DR   HOGENOM; CLU_059167_1_0_5; -.
DR   Proteomes; UP000007307; Chromosome.
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   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, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007307};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        36..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..214
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
SQ   SEQUENCE   318 AA;  35836 MW;  63A5115E6657B2F1 CRC64;
     MLLTTSKACS PTCPWPERVA RKLEAGGSMK LSLARLALLG AIVFGLVTLA LESAFIVDEA
     HQAIVVQFGR VQKSVQKSGL FYKVPVISEV IYFDKRIIEI RSDSCEVIAA DQKRFVVDFY
     AKYKIIDPVK FYQTVRSETG LENRLGSIIE SSLRAQVGSV ALINFLNEAR ADVMRRIQEG
     VSTESEKFGV EMVDVRIKRA DLPEENSAAI FRRMQTDREK EAREIRAEGE EMSQKIRSDA
     DFQTRVIIAD AMRDAQIIRG TGDAKASQIY NNALKADPDF FSFYRTMRAY RRVFSDGTTK
     IVLSPNNDFI SLFNKSRG
//
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