ID A0A0M4TYK4_9NOSO Unreviewed; 998 AA.
AC A0A0M4TYK4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peptidase C39 {ECO:0000313|EMBL:ALF56019.1};
GN ORFNames=ACX27_29300 {ECO:0000313|EMBL:ALF56019.1};
OS Nostoc piscinale CENA21.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=224013 {ECO:0000313|EMBL:ALF56019.1, ECO:0000313|Proteomes:UP000062645};
RN [1] {ECO:0000313|Proteomes:UP000062645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA21 {ECO:0000313|Proteomes:UP000062645};
RA Leao T.F., Leao P.N., Guimaraes P.I., de Melo A.G.C., Ramos R.T.J.,
RA Silva A., Fiore M.F., Schneider M.P.C.;
RT "Genome Of Nitrogen-Fixing Cyanobacterium Nostoc piscinale CENA21 From
RT Solimoes/Amazon River Floodplain Sediments And Comparative Genomics To
RT Uncover Biosynthetic Natural Products Potential.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALF56019.1, ECO:0000313|Proteomes:UP000062645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA21 {ECO:0000313|EMBL:ALF56019.1,
RC ECO:0000313|Proteomes:UP000062645};
RX PubMed=27034496;
RA Leao T., Guimaraes P.I., de Melo A.G., Ramos R.T., Leao P.N., Silva A.,
RA Fiore M.F., Schneider M.P.;
RT "Draft Genome Sequence of the N2-Fixing Cyanobacterium Nostoc piscinale
RT CENA21, Isolated from the Brazilian Amazon Floodplain.";
RL Genome Announc. 4:0-0(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP012036; ALF56019.1; -; Genomic_DNA.
DR RefSeq; WP_062297735.1; NZ_CP012036.1.
DR AlphaFoldDB; A0A0M4TYK4; -.
DR STRING; 224013.ACX27_29300; -.
DR PATRIC; fig|224013.5.peg.7005; -.
DR OrthoDB; 516912at2; -.
DR Proteomes; UP000062645; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro.
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:0030253; P:protein secretion by the type I secretion system; 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; IPR010132; ATPase_T1SS_HlyB.
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 NCBIfam; TIGR01846; type_I_sec_HlyB; 1.
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 SMART; SM00100; cNMP; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 441..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..577
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 671..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..120
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 284..406
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 445..724
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 758..993
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 998 AA; 111110 MW; A1F959538F8EA982 CRC64;
MTYIKSAFQE FIADLAGFEQ LPAEVIVSIA EKLEAWRYRI GQKIIGNENI PPKVIFLYEG
QVRLLGYEPQ TQAAITLKLL KPGAAIGEIS FLRQVPCEVA IASTEVICLA LNLEEYSRLI
AEYPAFAHMR QNHRHICEVF SVLGVQVAKQ ANAVTNFLEL SEQALLNTQI QYLSPGKKSS
NQLDIDSIWF VSGGEVKNFP PGSRLDLNAG TIEVTGKNPA RLIGFAPGDL SFLDNYSQAE
EESIYDTQTN ITDELDIPYA PEEITAVDYP ASKKQKHLKY PFVRGSGEVN ATFACFQMLS
KHLQIPIRRE VVRRILSEQI KRQGSISFPA CAYIAELIGL KAQLVDLPAS TIERLPTPAL
IRYRSNFAVL YSADAHHVVV GVPSQGIVRC KPKELLANLE LEDGSYQPQM RVLLLSATKE
TPQERFGVSW FLPYLSRYRR VLIEVFIASF FVQLAQLANP LVIQLIIDKV IVQNSISTLN
VLGALLLVVG LFEAIIGTLR TYLFVDTTNR IDMGLGSQII DHLLRLPLRY FERRPVGELS
TRINELENIR QFLTGTALTV GLDALFSVVY IVVMLFYSWQ LTLVGLGTIP IFVVITLIAS
PTISKQLRNK AERNAETQSY LVEVMSGIQT VKAQNIELRS RFSWQERYAR YVGAGFKTVV
TSTLANSTSN FLNKLSSLLV LWVGAYLVLQ GELTLGELIA FRIISGYVTS PILRLAQLWQ
NFQETALSLE RLSDIVDTPE EGEADRGNIP LPAIDGTVKF DNVSFRFNPN GPLQLTNINL
EFTAGQFIGI VGQSGSGKST MMKLLLRLYD VESGRILIDG YDIAKVELYS LRRQIGVVPQ
ETLLFDGTVQ ENIALTNPEA TTEEIIEAAR VACAHEFIMG LPNGYNTRVG ERGAGLSGGQ
RQRIAIARSV LQRPKLLVLD EATSALDYPT ERQVCLNLAK AFQGSTVFFI THRLNTVSHA
DTIVVMDASR VIEQGSHQEL MAAKGHYSYL YQQQEVNL
//
