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Database: UniProt
Entry: W4ALR4_9BACL
LinkDB: W4ALR4_9BACL
Original site: W4ALR4_9BACL 
ID   W4ALR4_9BACL            Unreviewed;       738 AA.
AC   W4ALR4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Lantibiotic mersacidin transporter system {ECO:0000313|EMBL:ETT32423.1};
GN   ORFNames=C161_23339 {ECO:0000313|EMBL:ETT32423.1};
OS   Paenibacillus sp. FSL R5-192.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT32423.1, ECO:0000313|Proteomes:UP000019041};
RN   [1] {ECO:0000313|EMBL:ETT32423.1, ECO:0000313|Proteomes:UP000019041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT32423.1,
RC   ECO:0000313|Proteomes:UP000019041};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
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:ETT32423.1}.
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DR   EMBL; ASPR01000047; ETT32423.1; -; Genomic_DNA.
DR   RefSeq; WP_051447441.1; NZ_ASPR01000047.1.
DR   AlphaFoldDB; W4ALR4; -.
DR   MEROPS; C39.004; -.
DR   PATRIC; fig|1226754.4.peg.4730; -.
DR   Proteomes; UP000019041; 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:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd18555; ABC_6TM_T1SS_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; 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   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        175..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        402..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          22..145
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          178..458
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          494..727
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   738 AA;  83102 MW;  BB718C6297BC948A CRC64;
     MPERPVFRLR RKRQRKIPVK LQMNQYDCGP SCLHMLLAYH GYEADFTDLR ERFAMLGNGR
     DGSSMLKMKE VAQTYHLKGI AKKAPVESLN NDFLPVICFW EDNHFVVLER IKTSGHFIIV
     DPALGRLVIS TQEFAEKYSG IFLLVYPDEG FVPLSEKKIS KVAYFKDLIR SNKKYFGWTV
     LLALGLQLVS VAFPFLMQVS IDAATSGEGY SLFPVLITSI VLLTLFQIGF SYMKDMCIVR
     LQELLDSQLT TNFVSHMLKL PYQYFEIRSR GDLMLRINSN TTIREILSQK MISTLINLFL
     IVVTFTYIVI QSRLIAFTLL GVGLVQILVF VYTRSRFKKL TQTQIVAQSL AGSFMTEVLE
     GISTIKSLGI EERTGEKWRA LFMRQLATVK EKAIFQTRVN TVTNTLSFMT PMLILLVGLY
     QIMQGNMTLG MLVSFQSLAA LFLGPLNSLA LMLNEFVMAD ALLDRIYDVI QAEESNKFKK
     KTPTLRDVKL NGDITIDQVS FRYTDYGEDV LKNINITIKA GQRVALVGKS GSGKSTLAKL
     LVGLYTPTQG NIYFDGVVVE ELEQQDIRSQ ISIVLQDNFV FNNTVYDNIR LHAEGSTLED
     VMFAAKLADI HDDIEKMPMK YNTLISEAGS NLSGGQKQRV ALARALVSRP KVLLLDEATS
     ALDTVTEATI AHNLNMLKCT QIIIAHRLST IRSADTIYVL DQGVLVDAGT HDELIGRCKS
     YNDLVCEQLD ETGARQYG
//
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