ID A0A1H7G0Y6_9BURK Unreviewed; 719 AA.
AC A0A1H7G0Y6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Colicin V processing peptidase. Cysteine peptidase. MEROPS family C39 {ECO:0000313|EMBL:SEK31829.1};
GN ORFNames=SAMN05216359_101408 {ECO:0000313|EMBL:SEK31829.1};
OS Roseateles sp. YR242.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1855305 {ECO:0000313|EMBL:SEK31829.1, ECO:0000313|Proteomes:UP000198631};
RN [1] {ECO:0000313|EMBL:SEK31829.1, ECO:0000313|Proteomes:UP000198631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR242 {ECO:0000313|EMBL:SEK31829.1,
RC ECO:0000313|Proteomes:UP000198631};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOAV01000001; SEK31829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7G0Y6; -.
DR STRING; 1855305.SAMN05216359_101408; -.
DR OrthoDB; 8554730at2; -.
DR Proteomes; UP000198631; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..139
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 174..452
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 487..719
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 719 AA; 79080 MW; 5078CF5299896A33 CRC64;
MMALLNLNFW QRQSLPIILQ TESAECGLAC LCMIASFWGR RMDLRTLRSR YPVSLKGATL
KQLMSTASEI QLVSRPLKLD MSYLPSLKTP CILFWDLNHF VVLKEVRRQA AVIHDPRIGS
RTLTLDEVSS HFTGVALELS PTSDFHSKDE RQSVTLRSLI GNVTGLKRGL AQTLVLGVSL
QVCALVSPFY MQWMVDEALV AQDRDLAAVL ALGFLALLAT QSLMTAFRSW LISLLAANFN
FQWLGNAFSH LMLLPLSYFE KRHLGDIVSR FGSIQTIQKS ITTQAIEAVV DGILVTCVAT
LMLLYSPALT VVSCLTVAVY ATIRSLLFRS MRAATAEQIL HAAKQQTQLL ESARGVQAIR
LFDKVEERRA SWLSALADQT NAELRISRLT VSYQAGNNIL FGAERIGIIW YAAVLVMQGQ
LSVGMMLAFL SYKDQFSQRI ASLVDKAFDF RMMRLHAERV ADIVHTAPER MLAVTQVASI
DYASADVEFR NVSFRYGVGE APVLDGISLT IKAGQSVVFT GPSGCGKTTL VKLLLGLLEP
SEGEILVGGV PLNRAGLQRW RAAVGAVMQE DGLFAGSIAD NISFFDAESS AERVAAAAKR
ASLHAEIASM PMAYNTLIGD LGSGLSGGQR QRLLLARAFY KDPRILVLDE ATSHLDIWNE
QAVNQSIQQA RLTRIMVAHR PETITMAERV VVLHAGKVLE DVIRDQQPAV MEPGLHVAS
//
