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Database: UniProt
Entry: A0A2G4F4Q7_9CYAN
LinkDB: A0A2G4F4Q7_9CYAN
Original site: A0A2G4F4Q7_9CYAN 
ID   A0A2G4F4Q7_9CYAN        Unreviewed;      1006 AA.
AC   A0A2G4F4Q7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Type I secretion system permease/ATPase {ECO:0000313|EMBL:PHX56691.1};
GN   ORFNames=CP500_004150 {ECO:0000313|EMBL:PHX56691.1};
OS   Tychonema bourrellyi FEM_GT703.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Tychonema.
OX   NCBI_TaxID=2040638 {ECO:0000313|EMBL:PHX56691.1, ECO:0000313|Proteomes:UP000226442};
RN   [1] {ECO:0000313|EMBL:PHX56691.1, ECO:0000313|Proteomes:UP000226442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FEM_GT703 {ECO:0000313|EMBL:PHX56691.1,
RC   ECO:0000313|Proteomes:UP000226442};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PHX56691.1, ECO:0000313|Proteomes:UP000226442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FEM_GT703 {ECO:0000313|EMBL:PHX56691.1,
RC   ECO:0000313|Proteomes:UP000226442};
RA   Tett A., Armanini F., Asnicar F., Boscaini A., Pasolli E., Zolfo M.,
RA   Donati C., Salmaso N., Segata N.;
RT   "Draft genome sequence of the planktic cyanobacteria Tychonema bourrellyi
RT   isolated from alpine lentic freshwater.";
RL   Submitted (NOV-2017) 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:PHX56691.1}.
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DR   EMBL; NXIB02000014; PHX56691.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4F4Q7; -.
DR   OrthoDB; 516912at2; -.
DR   Proteomes; UP000226442; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd18782; ABC_6TM_PrtD_LapB_HlyB_like; 1.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd02259; Peptidase_C39_like; 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; 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; 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; 1.
DR   Pfam; PF03412; Peptidase_C39; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 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; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000226442};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        447..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        488..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        558..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        589..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..123
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          296..418
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          451..730
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          765..1000
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          232..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1006 AA;  111511 MW;  089CB135F25D069E CRC64;
     MTSSAVSLGQ IQDFLAQTTP FDRLSETALT ALVAKCQLLG YRTGQPLFER EKMPTQVAII
     YEGQARLLGF DQRSQRHVSL RLVQSQEILG WAGLLRGVPC ETAIASTDVI AIVIQTEDFL
     SVLEKQPKFG EAFREHCSLS EAFELLSLEL QRQADATSNL KEITMQAWQD AKVVNLPNGN
     KKSQELAKEL DSDRIWLVSS GVLGDFPTGS RLNIDSEAKS LKVEGRMGAR LVGFREPPEP
     PPETAAADPL NGSINEGIED LGKKRRIVFD DVTQAPPVPP EPRSDQPKDT KYPVFRGRGQ
     IDGPLACFQM LSKYFGIKFR RDIIRKVLEN QLKTAGSVTI QACGAIAQSI GLTPQLAQIP
     ADAINRIKAP VMIKWKDTFA IVYSITEQEL VVASPEEGLM RKRVPQFREI WGESGEVLLL
     QAPQQIDQKE QFSFWWFVPA LMEHKTVFIE VLFASFFVQV FGLANPLISQ IIIDEVLGKR
     NLDTLDVLGA FLLGVALFEG LLNGLRTFLF IDTSNRIDVK LSAEIIDHLL RLPQNYFDNR
     RVGDLVYKFS MMGQIREFMT GTALTVVLDA VFSVVYVAVM LSYSVQLTAV SLAVVPILAL
     MIVLINPLVL RLIKQRNNRF SDAQSYLVEV VSGIQTVKAQ NIELKSRWEW SSRYAKYITA
     SFKTIITGTT AGTVSAFLNQ VGNLAQLWVG AYLVLKNEMT LGQLIAFRII SGNVTGSLLR
     FVSVWQSFQE VSMSVDMLKD IVDTPTETSD EDRSNIPMPA IQGQVTYEEV SFRFLESGSL
     QLANVNLEFP PGSFVGIVGG SGSGKSTAMK LLQRLYPPLS GRIFVDGYDI AKVELYSLRS
     QLGVVLQDTL LFNCTVQENI ALSNPDASTD EIVRAAKLAV AHDFIMGLPA GYNTIVGERG
     SSLSGGQRQR LAIARTILQN PKLLILDEAT SALDYHSERQ VCNNLAEAFS GRTVFFITHR
     LTTIQNADVI IMMDQGAVVE QGTHKELMGL KGRYYCLFQQ QEASNT
//
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