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Database: UniProt
Entry: K9P4J2_CYAGP
LinkDB: K9P4J2_CYAGP
Original site: K9P4J2_CYAGP 
ID   K9P4J2_CYAGP            Unreviewed;       715 AA.
AC   K9P4J2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein {ECO:0000313|EMBL:AFY27474.1};
GN   OrderedLocusNames=Cyagr_0273 {ECO:0000313|EMBL:AFY27474.1};
OS   Cyanobium gracile (strain ATCC 27147 / PCC 6307).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Cyanobium.
OX   NCBI_TaxID=292564 {ECO:0000313|EMBL:AFY27474.1, ECO:0000313|Proteomes:UP000010388};
RN   [1] {ECO:0000313|Proteomes:UP000010388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27147 / PCC 6307 {ECO:0000313|Proteomes:UP000010388};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003495; AFY27474.1; -; Genomic_DNA.
DR   RefSeq; WP_015107933.1; NC_019675.1.
DR   AlphaFoldDB; K9P4J2; -.
DR   STRING; 292564.Cyagr_0273; -.
DR   KEGG; cgc:Cyagr_0273; -.
DR   PATRIC; fig|292564.3.peg.249; -.
DR   eggNOG; COG2274; Bacteria.
DR   HOGENOM; CLU_000604_95_3_3; -.
DR   OrthoDB; 516912at2; -.
DR   Proteomes; UP000010388; Chromosome.
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:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR022514; NHPM_micro_ABC1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_1_exporter.
DR   NCBIfam; TIGR03796; NHLM_micro_ABC1; 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; 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, ECO:0000313|EMBL:AFY27474.1};
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        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        384..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..129
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          160..418
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          480..713
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   715 AA;  78394 MW;  9E4C4BD6F1E30A9C CRC64;
     MKHTPTVLQM ETTECGAASL AVILQHHGRH VPMSQLRDAC CVSRDGTNAA AIQAAARLYG
     LEVDGFMAED TKDLRRWERP VILHWQFNHF LVLEGISGRN VMLNDPAIGR RRVTLAEFER
     SFTGVFLDLK PGSSFRRGGH PPRFWGAIAQ RLALEKAGVL FTLITGLLLV LPQVLIPVFS
     QVYIDEIWGQ GMQAWLKPML WALVLVLLLQ TLLKHLQLTA IRRLTRRLDS RFSAQFERHV
     LSLPERYFSQ RYAGDINGRV ELNREVASFL AEQLIPLLSG VMLLVFYLVL TLSYSPWLGG
     VVGISTGLNA LLVAFTHHAH QEDSLRLQQD GAKAQSVVTA AIRDIETVKT AAVETDLATR
     YGGHLSTALN GSQRIGLRQA RLELVPGLLN QVNNLAVLIV GFVLLLRGEM TLGMVLAAQQ
     VSGGLKGEVD RWVAFVRELP TMQASLLRLE DVLGEPVDPL VNGRLCSMDS EGGSRLSGAI
     TLEAMSFGYI PTQQPLLGPI DLRVAPGQRL ALVGGSGSGK STLARLLAGL ERPDVGEILY
     DGHALEAIPR SVAVGSIALV QQEVQLYGVS VRDNLTLWNQ AIPHEQLEEA CRDAQILDDI
     RKLPQGFDTL LSEGGQSLSG GQRQRLEIAR ALVQNPAILI LDEASSALDA ITEQRLSEAL
     RRRGCTQIVI AHRLSAIRDA DQILVLEHGR VVQRGRHEDL LTDSSGVYAG LVADE
//
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