ID U2JCK1_9STRE Unreviewed; 796 AA.
AC U2JCK1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=ABC-type bacteriocin transporter {ECO:0000313|EMBL:ERJ77505.1};
GN ORFNames=HMPREF1557_00754 {ECO:0000313|EMBL:ERJ77505.1};
OS Streptococcus sobrinus W1703.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1227275 {ECO:0000313|EMBL:ERJ77505.1, ECO:0000313|Proteomes:UP000016617};
RN [1] {ECO:0000313|EMBL:ERJ77505.1, ECO:0000313|Proteomes:UP000016617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1703 {ECO:0000313|EMBL:ERJ77505.1,
RC ECO:0000313|Proteomes:UP000016617};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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:ERJ77505.1}.
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DR EMBL; AWVA01000046; ERJ77505.1; -; Genomic_DNA.
DR AlphaFoldDB; U2JCK1; -.
DR MEROPS; C39.001; -.
DR PATRIC; fig|1227275.3.peg.665; -.
DR HOGENOM; CLU_000604_84_3_9; -.
DR Proteomes; UP000016617; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043214; F:ABC-type bacteriocin 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 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; IPR005897; Pept_C39_ABC_bacteriocin.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR NCBIfam; TIGR01193; bacteriocin_ABC; 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:0000256|ARBA:ARBA00022807};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000256|ARBA:ARBA00022807};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..218
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 251..530
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 564..796
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 796 AA; 89093 MW; E7ED1A07DC6BB7B9 CRC64;
MPCSLFGVGD IFLKSSSTIF TGWLERNLMK QITYIILIVA LVIAVNIILE AFRRYFRSKR
GKSSPQSSQA VAGSSSSVGL FWRRRYKFIP QVDTRDCGPA ALASVAKHYG SDYSLARLRE
LSKTDKQGTT ALGLVEAAKA IGFETRSIKA DMTLFDYTDL TYPFIVHVVK NKRLQHYYVV
YGNDKNNLII GDPDPNVKVT RMSKQDFQEE WTGLAIFLAP TPNYKPKKDE KNGLMSFFPI
ILRQKALLTY IVLASLMVTL IDIVGSYYLQ GMLDEYIPDQ LISTLGIITI GLIITYIIQQ
MMSFAKEYLL NVLSLRLVID VILSYIKHIF TLPMSFFATR RTGEITSRFS DANQIINAVA
STIFSIFLDV TMLILVGGVL LVQNNHLFLL TLISIPIYAI IITAFLKPFE KMNHEVMEAN
AMVSSSIIED INGMETIKSL TSESSRYQNI DGEFVDYLEK NFKLQKMNAL QTSLKTGAKL
ILNVVILWYG ARLVMDGKIS VGQLITFNAL LSYFQNPIEN IISLQTKLQS ARVANTRLNE
VYLVESEFEN DGELSEDSFL DGDISFEKLS YKYGYGRDTL SDINLTIAKG SKVSLVGPSG
SGKTTLAKMM VNFYDPNRGI ARINGYDLKV IDKTALRQHI SYLPQQAYVF SGTIMDNLTL
GAKEGTTQED IIRACEIAEI RSDIEQMPLG YQTELSDGAG VSGGQKQRIA LARALLTQAP
VLILDEATSS LDVLTEKKIV DNLMAMTDKT VIFVAHRLSI AQRTDRIIVM DQGKIVEEGS
HKELLANKGF YYTLFN
//
