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Database: UniProt
Entry: A0A143X1L2_9FIRM
LinkDB: A0A143X1L2_9FIRM
Original site: A0A143X1L2_9FIRM 
ID   A0A143X1L2_9FIRM        Unreviewed;       487 AA.
AC   A0A143X1L2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Lipid II flippase FtsW {ECO:0000313|EMBL:CVH76535.1};
GN   Name=ftsW_2 {ECO:0000313|EMBL:CVH76535.1};
GN   ORFNames=BN3662_01633 {ECO:0000313|EMBL:CVH76535.1};
OS   Clostridiales bacterium CHKCI006.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1780379 {ECO:0000313|EMBL:CVH76535.1, ECO:0000313|Proteomes:UP000198633};
RN   [1] {ECO:0000313|EMBL:CVH76535.1, ECO:0000313|Proteomes:UP000198633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHKC6 {ECO:0000313|EMBL:CVH76535.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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; FCNA01000087; CVH76535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143X1L2; -.
DR   STRING; 1780379.BN3662_01633; -.
DR   Proteomes; UP000198633; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR001182; FtsW/RodA.
DR   PANTHER; PTHR30474; CELL CYCLE PROTEIN; 1.
DR   PANTHER; PTHR30474:SF1; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE MRDB; 1.
DR   Pfam; PF01098; FTSW_RODA_SPOVE; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198633};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        101..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        396..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        427..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        465..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   487 AA;  53541 MW;  EB195F3BC77CF20C CRC64;
     MLHFLESVIL LLLMGCMLHL MKERKDWTFG LKTDRLDGSQ GLETTVGRLG IHDIVDRSGQ
     TSRMQGSAFY DIKHRTIQWQ GKPVPISFGL PERYPLLDHH YLPLLLTSAF LILRMVELGQ
     PALFGMLMLY VIVMNGLKAD HMALADCIFV ILLSFHIQAS SHPYLGVIGY LASSILIRIV
     IQVTRRAEWH QWLRRIAALG ILLLIGMNIL LASKINGAYN WVTIGGVQFQ PSEIVKILYL
     FILVVPAGHH LGERGEQILI LSMTLIGFLY AYLIRDIGLL VQLGALFMVA VLVQNHALLL
     SITLILLALL VLKLLPQLSA EVAERLSGWL GGSLLSSLTA GGSFLDASNY GYQSVHAIVA
     FFVNGGLFGN PKLDILQNIT ASHSDLVVAW LGQMNGFILM MEVLGLEVLL LFHVLQKFKE
     ERRQNQVFSL LGCLGIMVAV CLNVGGTFSI IPLTGVVNPA LSNGISASIS YGAMFGLAAY
     SDLVITT
//
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