MCHF_ECOLX
ID MCHF_ECOLX Reviewed; 698 AA.
AC Q9EXN5; Q2WEK5;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable microcin-H47 secretion/processing ATP-binding protein MchF;
DE EC=3.4.22.-;
DE EC=7.-.-.-;
GN Name=mchF;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H47;
RX PubMed=11181394; DOI=10.1128/aac.45.3.969-972.2001;
RA Azpiroz M.F., Rodriguez E., Lavina M.;
RT "The structure, function, and origin of the microcin H47 ATP-binding
RT cassette exporter indicate its relatedness to that of colicin V.";
RL Antimicrob. Agents Chemother. 45:969-972(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H47;
RX PubMed=15047525; DOI=10.1128/aac.48.4.1235-1241.2004;
RA Azpiroz M.F., Lavina M.;
RT "Involvement of enterobactin synthesis pathway in production of microcin
RT H47.";
RL Antimicrob. Agents Chemother. 48:1235-1241(2004).
CC -!- FUNCTION: Probably involved, in conjunction with MchE, in the secretion
CC of microcin H47.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ009631; CAJ44959.1; -; Genomic_DNA.
DR RefSeq; WP_001529577.1; NZ_WSWV01000106.1.
DR AlphaFoldDB; Q9EXN5; -.
DR SMR; Q9EXN5; -.
DR MEROPS; C39.005; -.
DR PRIDE; Q9EXN5; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043213; P:bacteriocin transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02419; Peptidase_C39C; 1.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR033838; CvaB_peptidase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 3: Inferred from homology;
KW ATP-binding; Bacteriocin transport; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Protease; Protein transport; Thiol protease;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..698
FT /note="Probable microcin-H47 secretion/processing ATP-
FT binding protein MchF"
FT /id="PRO_0000092490"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 289..311
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 315..337
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 26..145
FT /note="Peptidase C39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT DOMAIN 176..458
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 492..698
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT ACT_SITE 32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT BINDING 526..533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 698 AA; 77851 MW; CEC8736DA319C520 CRC64;
MTNGSFRQII NQLDMRWRRR VPVIHQTETA ECGLACLAMI CGHFGKNIDL ISLRRKFNLS
ARGANLAGIN GIAEQLGMVT RALSLELDEL GALKMPCILH WDFSHFVVLV SVKRNRYVLH
DPARGRRYLG REEMSRYFTG IALEVWPGSE FLAETQQIRI SLRSLINSIY GIKRTLAKIF
CLSVVIEAIN LVMPVGTQLV MDHAIPAGDR GLLTLISAGL MFFILLRAAV SMLRAWSSLV
MSTLINIQWQ SGLFNHLLRL PLAFFERRKL GDIQSRFGSL DTLRATFTTC VVGAIMDSIM
VVGVFVMMLL YGGYLTWIVL GFTMVYVLIR LVTYGYYRQI SEETLVRGAR ASSYFMESLY
GIATVKIQGM AGIRGTHWLN LKIDAINSGI KLTKMDLLFG GINTFVAACD QVAILWLGAS
LVIDNQMTIG MFVAFGSFRG QFSDRVASLT SFLLQLRIMS LHNERIADIA LHEKEEKKPE
IEIVADMSPV SLETTDLSYR YDSQSAQVFS GLNLSVAPGE SVAITGASGA GKTTLMKVLC
GLFEPDSGKV LVNGTDIRQL GINNYHRMIA CVMQDDRLFS GSIRENICGF AEETDDEWMT
ECARASHIHD VIMKMPMGYE TLIGELGEGL SGGQKQRIFI ARALYRKPGI LFMDEATSSL
DTESERFVNA AIKKMNITRV IIAHRETTLR TVDRIISI
