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Database: UniProt
Entry: A0A0U2VGQ9_9ENTE
LinkDB: A0A0U2VGQ9_9ENTE
Original site: A0A0U2VGQ9_9ENTE 
ID   A0A0U2VGQ9_9ENTE        Unreviewed;       705 AA.
AC   A0A0U2VGQ9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=ABC transporter ATP-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ATZ35_05795 {ECO:0000313|EMBL:ALS36683.1};
OS   Enterococcus rotai.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=118060 {ECO:0000313|EMBL:ALS36683.1, ECO:0000313|Proteomes:UP000067523};
RN   [1] {ECO:0000313|EMBL:ALS36683.1, ECO:0000313|Proteomes:UP000067523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26678 {ECO:0000313|EMBL:ALS36683.1,
RC   ECO:0000313|Proteomes:UP000067523};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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; CP013655; ALS36683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U2VGQ9; -.
DR   STRING; 118060.ATZ35_05795; -.
DR   Proteomes; UP000067523; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03228; ABCC_MRP_Like; 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; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
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; 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; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000256|ARBA:ARBA00022807};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        179..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        394..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        433..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..135
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          489..705
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   705 AA;  80262 MW;  1B1CBE358772CE9B CRC64;
     MYAHYMQHST TDCGIASLKT ILKQLRIKIG NENELYQHYS IKKTQGLSLD EMKTILKKYG
     VNSSAYGVTD FEKLKKVEKL PMLLVVENDG VGHYIVVHEI KDNQSFIVSN PAERTLIEYD
     EAYLKSIFLG YALCIADSNS LVTNRSKMKF RMNKVESSLG KRLYKEVMQE ISYSLKVKMI
     GLILLKYLLP IVTTFLIQGT LSLNRTDSAP MFVFVISVAL LLILGFYKIN IMEGKQKVTL
     ENKIQEKILM KYYVQKVSDI KSGGNSDNVT GYFWNLFGSV SGLLEKFYFK LNLVYVLLLA
     SIVFSITPLL FGVLVFWIGL FSYFLKRKID IIRNNEKDVI GKSSAFSFSV ENNIKSSFDI
     NLFSKNKEAE SFVQQKIQDY FESKNQMVTN DLKIASMFQV FSTLISISTF VVFGVNAALH
     TGSTTSLLND SNGILIISII LSSVAPVLQS WLSYQKSAIA IDYIQSGEDY TEQAEKSEDV
     LDVPKITTID VKNLNFSYDE KKTIFKQFDT RFEAGKLYTL IGDNGCGKST LINLLSGVLD
     PDSGTMIVNE SVEKSSFKNT NIREYISLYS PEFNLYGNTV GRNIRYKVFN EPLTTEEKSH
     YDDLLDLKLP NSYFIQSEGR NLSQGQKQKI LLMRALYQDT SLYIFDEPTG NLDSASKKKF
     MNYIKKLAND EKKIVIVISH ETDVLEYADE IINIKEKRRG DKNEK
//
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