ID A0A2T1M0B2_9CHRO Unreviewed; 1007 AA.
AC A0A2T1M0B2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Type I secretion system permease/ATPase {ECO:0000313|EMBL:PSF38114.1};
GN ORFNames=C7H19_06485 {ECO:0000313|EMBL:PSF38114.1};
OS Aphanothece hegewaldii CCALA 016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=2107694 {ECO:0000313|EMBL:PSF38114.1, ECO:0000313|Proteomes:UP000239001};
RN [1] {ECO:0000313|EMBL:PSF38114.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF38114.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSF38114.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF38114.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Keele B.F.;
RL Submitted (MAR-2018) 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:PSF38114.1}.
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DR EMBL; PXOH01000005; PSF38114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1M0B2; -.
DR OrthoDB; 9762778at2; -.
DR Proteomes; UP000239001; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000239001};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 456..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 592..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..140
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 302..424
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 456..733
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 767..1002
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1007 AA; 113179 MW; 4456DB343EEFD716 CRC64;
MRESFEITET TETIQDFLGN VFPFNSLDQA TLFKLAEQMK PLRYSMGQTI MAQGKMSPYI
VILYEGKARW LSYDPCQQTS VTLKILEPGA IIGCVNWARK QPCEAASAST EVVGLTLSYQ
AFLKLLEQHP QLATELFEQI SILEVFDLLG YHLAQQAKVV KNLLKLTQEI LPSTRILSVP
ANTRLKLKQS PLGDPNWVWL VSGGGQVLGF PIGSRFNPTT EEITLRVSDS EAIRFLAIPQ
EQWSRIVELQ TEQNHNNNHQ SNNKYLITEQ AISAPNELLE DTSLSDFITH NPKNRINSAY
ISGKGSLKAA MACFQMISRY FNVSFSRETV RNILNKKLQL HGVISLDICE LIAESMGLKT
QLITVPSSNL RRLKLPGMMI KNEKLIILYE IGDQVVMIGQ PGKGLTRRST DEFFSGLNEE
VQILLLSEMQ KREKEPFGLR WFFPTLMRYR WKLIEVLLAS FVVQILGLVF PLTIRFLIDK
GDGSVANLNI IGFLLLGVAI FETLLTMARD NLLSDTTNRI DMSMGTNAIN HLFHLPLNYF
QRHPIGQITS RVNELEDVRE FLTGQALRAI IDTALSIVLI AVLALLSPLL TVLVLAVIPL
SIILTIAFSP ATRQRLRYKA EQKSLVQSHL VETITGIETV KCQSLELPMR WRWQDNYADY
ISASVDAAEI ASLSRTFNNF LQQLSRLMIV WVGFYLVFTG QLTLGTLIAI RIIAGQVTSP
ILRLSQIWQN FQKTTLSLER LGEFMNLPAE GEQDYDNIPM PVIKGTVSFE DVSFRHQSSG
AFQLNKINLT IPMGTSVALV GGSGAGKSTL MDLLARLYKP EFGRIVIDGY DINKVELFSL
RQQISIVPQE TMLFEGSIKD NLSMTNPNAT SEEIVRAAKI AVAHDFIMNL PNGYNTMIGE
KGSTLSGGQR QRLVIARAIL QQPRILVLDE ATSALDYTTE QQILLNLQEI FTEQTIFYIT
HRLDTIKNAD LIIVMKNGAV VEQGIHEELI NLKGHYYGLN QRQESLA
//
