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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//