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Database: UniProt
Entry: W0HUC1_9GAMM
LinkDB: W0HUC1_9GAMM
Original site: W0HUC1_9GAMM 
ID   W0HUC1_9GAMM            Unreviewed;       698 AA.
AC   W0HUC1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Colicin V secretion/processing ATP-binding protein {ECO:0000313|EMBL:AHF77426.1};
GN   Name=cvaB {ECO:0000313|EMBL:AHF77426.1};
GN   ORFNames=Sant_2382 {ECO:0000313|EMBL:AHF77426.1};
OS   Sodalis praecaptivus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF77426.1, ECO:0000313|Proteomes:UP000019028};
RN   [1] {ECO:0000313|EMBL:AHF77426.1, ECO:0000313|Proteomes:UP000019028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1 {ECO:0000313|EMBL:AHF77426.1,
RC   ECO:0000313|Proteomes:UP000019028};
RX   PubMed=24407854; DOI=10.1093/gbe/evt210;
RA   Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA   Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA   Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT   "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL   Genome Biol. Evol. 6:76-93(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP006569; AHF77426.1; -; Genomic_DNA.
DR   RefSeq; WP_025422567.1; NZ_CP006569.1.
DR   AlphaFoldDB; W0HUC1; -.
DR   KEGG; sod:Sant_2382; -.
DR   PATRIC; fig|1239307.3.peg.2648; -.
DR   HOGENOM; CLU_000604_84_3_6; -.
DR   OrthoDB; 6828292at2; -.
DR   Proteomes; UP000019028; Chromosome.
DR   GO; GO:0016020; C: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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd18567; ABC_6TM_CvaB_RaxB_like; 1.
DR   CDD; cd02419; Peptidase_C39C; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF606; COLICIN V SECRETION-PROCESSING ATP-BINDING PROTEIN; 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; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:AHF77426.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019028};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        171..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..145
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          179..458
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          492..698
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   698 AA;  77154 MW;  8060FF03E2EDDF2D CRC64;
     MNPKKWDRLR ENLDIGFFKR VPLVHQTETA ECGLACLSMI CGYYGNPVDL ISLRHRCSLS
     SRGATLAGIE RIAGQLEMVT RALSLELEDL PRLKLPCILH WDFSHFVVLV KARRQRLIIH
     DPARGRRSIP LNVLAKHFTG VALEVWPGSH FTAKTPSPGL RLRALIRGVK GLVPALIKIG
     CLSLVIETIN LLMPVGTQLV MDQVVPAGDG GLLMLICTGL LVFILLRTAI GLIRAWSSLV
     MGTLIDVQWK AGLFSHLLTL PITYFERRKL GDIHARFASL DVLRATFTKS VVGAVMDGMM
     VAGAAAMMVF YGGHLVWVVG GFSLLYIGIR FATYDSYRQL SQDELVRDAR ANSYFMETLY
     GIQTIKMQGM AERRRTCWLN LTIDKINTQI KVSKMTLFFD GVNGFINACE QVIILWLGTR
     LVIDNRMTLG MMVAFGAFRA QFSDRTASLI SFVLQLRMMG LHNERIADIA LHAPAPSGAL
     LSAHAFSGPV SLTADKIGYR YDSQSPPVFS QVDFRIAPGE SVAIAGPSGA GKTTLVKVLC
     GLFPPDTGTI KVNDIDIYRL GLNHYHQMIA CVMQDDKLFS GSLRENICGF GPCEDEAWMI
     ACARAGHIHE TIMAMPMGYD TTIGELGEGL SGGQKQRVFI ARALYRKPAI LFMDEATSHL
     DKSSEEAVNQ AIKTMRITRV IIAHRESTLR SADRILTL
//
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