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Database: UniProt
Entry: A0A3S1AHV4_CHLFR
LinkDB: A0A3S1AHV4_CHLFR
Original site: A0A3S1AHV4_CHLFR 
ID   A0A3S1AHV4_CHLFR        Unreviewed;       716 AA.
AC   A0A3S1AHV4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Bacteriocin cleavage/export ABC transporter {ECO:0000313|EMBL:RUR80233.1};
GN   ORFNames=PCC6912_30930 {ECO:0000313|EMBL:RUR80233.1};
OS   Chlorogloeopsis fritschii PCC 6912.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Chlorogloeopsidaceae;
OC   Chlorogloeopsis.
OX   NCBI_TaxID=211165 {ECO:0000313|EMBL:RUR80233.1, ECO:0000313|Proteomes:UP000268857};
RN   [1] {ECO:0000313|EMBL:RUR80233.1, ECO:0000313|Proteomes:UP000268857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6912 {ECO:0000313|EMBL:RUR80233.1,
RC   ECO:0000313|Proteomes:UP000268857};
RX   PubMed=30590650;
RA   Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA   Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA   Neumann-Schaal M., Petersen J.;
RT   "Day and night: Metabolic profiles and evolutionary relationships of six
RT   axenic non-marine cyanobacteria.";
RL   Genome Biol. Evol. 0:0-0(2018).
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:RUR80233.1}.
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DR   EMBL; RSCJ01000011; RUR80233.1; -; Genomic_DNA.
DR   RefSeq; WP_016873902.1; NZ_RSCJ01000011.1.
DR   AlphaFoldDB; A0A3S1AHV4; -.
DR   STRING; 211165.GCA_000317285_01353; -.
DR   OrthoDB; 437054at2; -.
DR   Proteomes; UP000268857; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd18570; ABC_6TM_PCAT1_LagD_like; 1.
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; 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; 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; PF00664; ABC_membrane; 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; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268857};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        162..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        389..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..130
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          166..447
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          482..716
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   716 AA;  79373 MW;  27E01DD2AC597B4A CRC64;
     MKYKIVKQHS EEDCGAACIA SVAKHYGRNF TLSHIREAVG TGQFGTTLLG LKRGAETLGF
     NARPVKTSPD ILNRIKEAPL PAIIHWQGNH WVVLYGKKGN KCVIADPAVG IRYLSKKEVA
     DNWTDWLMLL LQPDPIRFSA QKDDELGGFW RFFKRVWNFR GILAQALPLN LLLGVLSLAS
     PFLLQILTDD VLVRGDTRLL TTVAIAVVVM HFISKSLSFV QSNLIAHFAQ RLQLGLVLEF
     GRQILRLPLS YYEARRSGEI VSRLRDINQI NQLVSQVIIG LPSQFFIAVV SFGFMLFYSW
     KLTAVAIVIA LAMTISTILF LPTLRIKTRE LLVQEAEAQG VLVETFKGAI TLKTTTAAPQ
     FWDEFQSRFG RLATLTLNTM QIAIVNGTFS GFVAAIGGVI LLWFGGNLVI QPQENLSIGQ
     LLAFNAMNAN FLALISSVIS FVDEYTHAKT AVQRLTEVID ATPEDDEDGK KQFAKIPGDA
     DIICTNVNFH YAGRLDLLQD FSLTLPGGKV IALIGKSGCG KSSLAKLIAG LYQLQSGNIR
     IGLYNLDDLA LDCLRQQIVL VPQEAHFWSR SIVENFRLGT PHVLFEDIVK ACQIAEADEF
     ISKLPDKYQT ILGEFGANIS GGQRQRLAIA RAIVTDPPVL ILDESTAGLD PVSEAQVLDR
     LIEHRRGKTT ILISHRPRVI NRADWIVFLE QGKLKLQGSL EELRSINGAH LDFLIP
//
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