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Database: UniProt
Entry: Q5P6N2_AROAE
LinkDB: Q5P6N2_AROAE
Original site: Q5P6N2_AROAE 
ID   Q5P6N2_AROAE            Unreviewed;      1021 AA.
AC   Q5P6N2;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   SubName: Full=Probable fusion of ABC transporter-type transmembrane and ATP binding protein {ECO:0000313|EMBL:CAI07029.1};
GN   ORFNames=ebA1666 {ECO:0000313|EMBL:CAI07029.1};
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI07029.1, ECO:0000313|Proteomes:UP000006552};
RN   [1] {ECO:0000313|EMBL:CAI07029.1, ECO:0000313|Proteomes:UP000006552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1 {ECO:0000313|EMBL:CAI07029.1,
RC   ECO:0000313|Proteomes:UP000006552};
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CR555306; CAI07029.1; -; Genomic_DNA.
DR   RefSeq; WP_011236754.1; NC_006513.1.
DR   AlphaFoldDB; Q5P6N2; -.
DR   STRING; 76114.ebA1666; -.
DR   KEGG; eba:ebA1666; -.
DR   eggNOG; COG0664; Bacteria.
DR   eggNOG; COG2274; Bacteria.
DR   eggNOG; COG2905; Bacteria.
DR   HOGENOM; CLU_000604_95_3_4; -.
DR   OrthoDB; 8554730at2; -.
DR   Proteomes; UP000006552; Chromosome.
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:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd18568; ABC_6TM_HetC_like; 1.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd02418; Peptidase_C39B; 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; 2.60.120.10; Jelly Rolls; 2.
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; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF03412; Peptidase_C39; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
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; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000006552};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        461..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        502..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        572..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        603..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        681..703
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        715..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..123
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          152..263
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          313..432
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          468..744
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          780..1016
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   1021 AA;  113784 MW;  31FF04B9A42DCFDF CRC64;
     MSTDAPPKLD SLADFLSSVE LLSPFTRDEL EQLAGQAQPR FLAFGETVCS AGEPADGVFV
     IRSGSVRIFA DEHGKEISLG VRKARETVAE MAMLREYRHE FSARASAKTE LLLIPRQAFE
     PVLAKNPAAQ AFVTSYVAIG SAGGVVARLF DLRGKVDRAE LEELVRSVGV KRVAAGREIL
     KQDARDDRRL YVVRQGEVRL VRTEQGSEYP LATLGHGEIF GEKACLMRQE QVASVVAVVD
     TTLLVVPEKS VHQILERNPK LREVLEERIR FVERELQRQK KLAERRNLRV MLDLQSKPEL
     GERLIRRFPL VEQAEEMDCG AACLAMICRH YDIPMTLGKL RELANVTTQG ATLDSLARAG
     ESLGFTTRGV QCTFDALLGF ELPFIVHWEG YHYVVVYGVS KRQVWVADPA VGFRKIAIEE
     FERGWSGTCL LFTPGQNLAQ LTVSRSPWLR FVSYLRPYKK ILAHLVMATF VIQVLGIVPP
     LIIQNILDGV IVHENVSLLH LLIAGLVITN LFTLLMSGIR AFLANFMVRN MDFAMMSQFF
     KHTLSLPFSF FAKRKTGDIF ARFQENQTIR AFLTESTVTT VLNLLMVFIY FTILFLYNVK
     MTLLLLAFVI PIMALTVLVT PKIKNYAREV FTTSTDAKAF LMEALGGVET VKGMGIERPV
     RLKWEKKYAK ALEVQYRAQR FNVLVGVASQ VLNAATTIAI LWVGASQVLA HQLTIGQLIA
     FNALMGSVLA PLMGLVALWS QVNDAGVAME RLGDVLDMEP EQRPEEVASR VVLPDLQGHI
     AFEGVYFRYG GDETPYVLEN ISFEIKPGEL VAIVGRSGSG KTTLAKLLVG FYPPTDGRIV
     VDGYDMATID KEYYRAQVGY VMQSNLLFSG TIAENIASGD EAPDRRRIEE VARMADAHAF
     IRKMPLGYEQ IVGERGVGLS GGQIQRLCIA RALYHDPRLL VFDEATSALD TQSESNIISN
     MHDILAGRTA VVIAHRLSTI MRADKILVLY EGAIVEQGRH DELVDRRGMY YQLVQKQLAA
     A
//
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