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Database: UniProt
Entry: A0A0A2WJX7_9GAMM
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ID   A0A0A2WJX7_9GAMM        Unreviewed;       702 AA.
AC   A0A0A2WJX7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Colicin V secretion ABC transporter ATP-binding protein {ECO:0000313|EMBL:KGQ18555.1};
GN   ORFNames=LF41_581 {ECO:0000313|EMBL:KGQ18555.1};
OS   Lysobacter dokdonensis DS-58.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ18555.1, ECO:0000313|Proteomes:UP000030518};
RN   [1] {ECO:0000313|EMBL:KGQ18555.1, ECO:0000313|Proteomes:UP000030518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-58 {ECO:0000313|EMBL:KGQ18555.1,
RC   ECO:0000313|Proteomes:UP000030518};
RA   Kim J.F., Kwak M.-J.;
RT   "Genome sequences of Lysobacter dokdonensis DS-58.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGQ18555.1}.
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DR   EMBL; JRKJ01000018; KGQ18555.1; -; Genomic_DNA.
DR   RefSeq; WP_036169848.1; NZ_JRKJ01000018.1.
DR   AlphaFoldDB; A0A0A2WJX7; -.
DR   STRING; 1300345.LF41_581; -.
DR   PATRIC; fig|1300345.3.peg.2250; -.
DR   eggNOG; COG2274; Bacteria.
DR   OrthoDB; 6828292at2; -.
DR   Proteomes; UP000030518; Unassembled WGS sequence.
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:KGQ18555.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030518};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        156..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        393..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..125
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          158..438
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          472..702
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   702 AA;  76346 MW;  51CA59E5E204BC82 CRC64;
     MNVIHQSESS ECGLACLAMV ASHHGQHVGL RELRRRFPLS LKGAPLSRLI TIAGDLGFQC
     RALRLELKDL SQLATPCVLH WDLNHYVVLA KVRGDKVTIY DPASAKLVLS LSEVSAHFTG
     VALELTPGAS FVRERAAPSV SVRQLSGRVT GLWRSLGLLL GLSVALQVCA LLAPFYMQWV
     VDHVLVAADR DLLTVLGLGF GLVVLLQVAM GALRGWSVVY LSTRLSLQWT GNIFAHLLRL
     PLDFFEKRHL GDITSRMGAV QAIQRTLTTS FVEALIDGLT ALVTLGMMLL YSWKLATATM
     LAVGLYLGVR AIAFRPLRDG TERQLVAAAR QETHLLESIR GVQSVKVAGS ESVRPSTFFN
     LMHDTANQDV RLAKLSLGFS SASQLIFGIE RVAVIWVGAA LALQNVFSVG MLVAYLAYRE
     QLAQRVSGLI DKWIEFRMLR LHGERLADIA LAEPEAETQP VSVSHDIQRA RLEVSGLSFR
     YAEGEPLVIH DCTFSVEDGE SVAIVGASGC GKSTLVKLLL GLLPPTQGTI AVDGNDLRKL
     GPAHFRQWVG AAMQDDQLFA GSIAENIAFG NDGYDLERVM QAAALAALHS DILGMPMGYH
     SLIGDMGTTL SGGQKQRVIL ARALYRRPRF LFLDEATSHL DVDCERQVND AVRGLPLTRV
     IIAHRPETIA SADRVLVMHS GQIVQELRPK AAPLSALASQ LA
//
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