ID A0A1I1JJN8_9GAMM Unreviewed; 718 AA.
AC A0A1I1JJN8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ATP-binding cassette, subfamily B, RaxB {ECO:0000313|EMBL:SFC48696.1};
GN ORFNames=SAMN02745724_01780 {ECO:0000313|EMBL:SFC48696.1};
OS Pseudoalteromonas denitrificans DSM 6059.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1123010 {ECO:0000313|EMBL:SFC48696.1, ECO:0000313|Proteomes:UP000198862};
RN [1] {ECO:0000313|EMBL:SFC48696.1, ECO:0000313|Proteomes:UP000198862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6059 {ECO:0000313|EMBL:SFC48696.1,
RC ECO:0000313|Proteomes:UP000198862};
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; FOLO01000010; SFC48696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1JJN8; -.
DR STRING; 1123010.SAMN02745724_01780; -.
DR OrthoDB; 9806127at2; -.
DR Proteomes; UP000198862; 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; 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; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:SFC48696.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198862};
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..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..140
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 174..453
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 487..716
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 718 AA; 80743 MW; 836EC78E81B71263 CRC64;
MDNVINKLSF SNKKKLPVLL QSEAAECGLT CICMIANYYG HKIDLFSLRR KYPISLKGAT
LKQLVNIAAQ LKMTGRALKV ELNQLKSLNT PVILHWDLNH FVVLKAVKRN GIIINDPAKG
EVFISMEVAS KSFTGIAMEI RPTDDFIEKD EELKLGLGVL WKSITGLKRS LAQVIVLSLV
LQFLALLAPY FIQLVVDNVV ITDDRRFLFV LGLGFSLLLL LKVATQAIRS WVVVYLRTTL
GIQLVSNLFR HMLRLPMSWF GKRFIGDITS RFNSLEYIKQ LLSGGFVEGI VDGMMAIITL
IMMYVFSPQL ALLTTTAFIF YTISRFALFQ PMRNHTKEKL QLKAVSDSLF YESVRSVQPV
KIFSGEAIRQ SKLENANADW MNADIKLGKL TIAYVTFKEL LHGMEYVLLI WIGAYLILDG
DMTVGILFAF LAYRQQFTTS AQILIEKLFE WRMMGLHLSR IADIALEEQE SALETEHPEL
ERVEGKIELK NVSYRYNDNE PYIFENLSLT IKSGECVALI APSGFGKTTL MKIIMGLLPP
STGSVLLDGK DILQIGLSNY RNVTSAVMQG DDLLSGSLGD NISFFSIEQD MERLEAVAKN
AFIYDDITAM PMGFHSLAGD MGSTLSGGQV QRILIARALY KDPKILFLDE ASSALDTQTE
RQINIALKNM GITRIMISHR QETINMADRI IDLSKLNNDD HQIKPESEST HSKLKIVK
//
