CVAB_ECOLX
ID CVAB_ECOLX Reviewed; 698 AA.
AC P22520;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Colicin V secretion/processing ATP-binding protein CvaB;
DE EC=3.4.22.-;
DE EC=7.6.2.-;
GN Name=cvaB;
OS Escherichia coli.
OG Plasmid IncFI ColV3-K30.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2249654; DOI=10.1002/j.1460-2075.1990.tb07606.x;
RA Gilson L., Mahanty H.K., Kolter R.;
RT "Genetic analysis of an MDR-like export system: the secretion of colicin
RT V.";
RL EMBO J. 9:3875-3884(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 373-698.
RX PubMed=9743528; DOI=10.1084/jem.188.6.1091;
RA Otto B.R., van Dooren S.J.M., Nuijens J.H., Luirink J., Oudega B.;
RT "Characterization of a hemoglobin protease secreted by the pathogenic
RT Escherichia coli strain EB1.";
RL J. Exp. Med. 188:1091-1103(1998).
CC -!- FUNCTION: Involved, in conjunction with CvaA, in the secretion of
CC colicin V.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Colicin V
CC exporter (TC 3.A.1.110.2) family. {ECO:0000305}.
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DR EMBL; X57524; CAA40744.1; -; Genomic_DNA.
DR EMBL; AJ223631; CAA11515.1; -; Genomic_DNA.
DR PIR; S12272; IKEC5B.
DR RefSeq; WP_000184924.1; NZ_WTCP01000077.1.
DR AlphaFoldDB; P22520; -.
DR SMR; P22520; -.
DR MEROPS; C39.005; -.
DR TCDB; 3.A.1.112.12; the atp-binding cassette (abc) superfamily.
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; Plasmid; Protease; Protein transport; Thiol protease;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..698
FT /note="Colicin V secretion/processing ATP-binding protein
FT CvaB"
FT /id="PRO_0000092238"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 211..231
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..334
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 412..432
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; 78246 MW; 47FC40510AF5D28A CRC64;
MTNRNFRQII NLLDLRWQRR VPVIHQTETA ECGLACLAMI CGHFGKNIDL IYLRRKFNLS
ARGATLAGIN GIAEQLGMAT RALSLELDEL RVLKTPCILH WDFSHFVVLV SVKRNRYVLH
DPARGIRYIS REEMSRYFTG VALEVWPGSE FQSETLQTRI SLRSLINSIY GIKRTLAKIF
CLSVVIEAIN LLMPVGTQLV MDHAIPAGDR GLLTLISAAL MFFILLKAAT STLRAWSSLV
MSTLINVQWQ SGLFDHLLRL PLAFFERRKL GDIQSRFDSL DTLRATFTTS VIGFIMDSIM
VVGVCVMMLL YGGYLTWIVL CFTTIYIFIR LVTYGNYRQI SEECLVREAR AASYFMETLY
GIATVKIQGM VGIRGAHWLN MKIDAINSGI KLTRMDLLFG GINTFVTACD QIVILWLGAG
LVIDNQMTIG MFVAFSSFRG QFSERVASLT SFLLQLRIMS LHNERIADIA LHEKEEKKPE
IEIVADMGPI SLETNGLSYR YDSQSAPIFS ALSLSVAPGE SVAITGASGA GKTTLMKVLC
GLFEPDSGRV LINGIDIRQI GINNYHRMIA CVMQDDRLFS GSIRENICGF AEEMDEEWMV
ECARASHIHD VIMNMPMGYE TLIGELGEGL SGGQKQRIFI ARALYRKPGI LFMDEATSAL
DSESEHFVNV AIKNMNITRV IIAHRETTLR TVDRVISI
