ID K9V7T2_9CYAN Unreviewed; 933 AA.
AC K9V7T2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Type I secretion system ATPase {ECO:0000313|EMBL:AFZ04128.1};
DE EC=3.6.3.43 {ECO:0000313|EMBL:AFZ04128.1};
GN ORFNames=Cal6303_5242 {ECO:0000313|EMBL:AFZ04128.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ04128.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ04128.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ04128.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003610; AFZ04128.1; -; Genomic_DNA.
DR RefSeq; WP_015200738.1; NC_019751.1.
DR AlphaFoldDB; K9V7T2; -.
DR STRING; 1170562.Cal6303_5242; -.
DR KEGG; calt:Cal6303_5242; -.
DR PATRIC; fig|1170562.3.peg.5742; -.
DR eggNOG; COG2274; Bacteria.
DR HOGENOM; CLU_000604_95_3_3; -.
DR OrthoDB; 9762778at2; -.
DR Proteomes; UP000010477; 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: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; cd18588; ABC_6TM_CyaB_HlyB_like; 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; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
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; 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 Hydrolase {ECO:0000313|EMBL:AFZ04128.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 377..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 234..353
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 381..660
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 693..928
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 933 AA; 103508 MW; D2BA97AAA70CE7BD CRC64;
MASREDSKVN GQAASRLTTA ADQEELRERV LASIPWDEAP FSCLSAQGQD LLRNNLEIRR
FAIGEKIWSK DIRGFQHFLV IGKVRLREEE TSIPLATLDA GDWFGDLLSS AVDCKANAAS
KEVIVASWIT SLWDEISTPE VRAFWESAES TAIASDSPSF GNAKGVMAPT RPEVIDLDGE
SPSQSEIYER QFAQDSIPIT PTTPVSSQKP QFQRELLIPS TSQDFSAYPF VGGQNTAAAC
LTMVAQQLQN PVQLELVQRQ LRGQKPKNLV ETADKLGFLL RRIQVSWVEM RQLSFPCLLY
LGATSEREGG WVVAFATKGE RLIVANPLNP EQVCENLSQL QLAEVWDGQL WQAELISKQE
KFNLGWFTPA VWRYKGLLTE VLIASFTLQL LGLTTPLITQ VVIDKVMVQE SLPTLDVMAI
ALLSVATFEA ALGILRLFIF THTARRLDLS LSAQLFRHLM RLPLAYFESR RVGDTVARVQ
ELEQIRQFLT GTALTVVLDS VFAVVYLALM FYYSIPLTAA ALAVLPLFAI LTLVATPILR
RWLNETFNRS ADSQSFLVET ITAIHSVKAH AAEPVARDRW EGLFARFIRT GFKASTTSNI
SSNIGDFLTN FSSLLILWFG AKLVIEQKLT VGQLVAFQML SGRVTGPLLR LVQLWQNLQQ
VLLSVDRIGD ILNVAPEAES GTGLVLPPLK GQVSFEQVFF RYKPENEPVL RGISFDVKPG
QFIGIVGRSG SGKSTLSKLL QRLYTIESGR ILVDGFDIKS ADLASLRQQI AVVLQEDFLF
NASILENITL GNPDISAEEV VQAARMAVAH DFISQQPQGY ETNVGERGTA LSGGQRQRIA
LARLFLSNAP VLVLDEATSA LDAETEQQVL QNLQKVSQGR TVFIIAHRFA PLKRADQIIV
MERGVIAERG THEGLLRDKG LYYSLYQRQQ ANI
//
