ID   FLP_STAAW               Reviewed;         498 AA.
AC   Q8NUZ4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Protein flp;
DE   AltName: Full=FmtA-like protein;
GN   Name=flp; OrderedLocusNames=MW2365;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Its precise function is unknown. Has no penicillin-binding
CC       activity and is not involved in methicillin resistance (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Has two of three conserved motifs typically found in
CC       penicillin-binding proteins (PBPs) and beta-lactamases, but no
CC       penicillin-binding activity has been detected. {ECO:0000250}.
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DR   EMBL; BA000033; BAB96230.1; -; Genomic_DNA.
DR   RefSeq; WP_000208557.1; NC_003923.1.
DR   AlphaFoldDB; Q8NUZ4; -.
DR   SMR; Q8NUZ4; -.
DR   MEROPS; S12.011; -.
DR   EnsemblBacteria; BAB96230; BAB96230; BAB96230.
DR   KEGG; sam:MW2365; -.
DR   HOGENOM; CLU_020027_4_2_9; -.
DR   OMA; KWQENYE; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..498
FT                   /note="Protein flp"
FT                   /id="PRO_0000087310"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        433..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   498 AA;  56557 MW;  AD82CBC49BCDE868 CRC64;
     MTTKKLYFLS ISIIILVAIS IAIHITLNSN TKTRLTNDSQ QQIDTIIEHD LQKGHIPGAS
     ILIVKNGKVF LNKGYGYQDV DKKVKASPTT KYEIASNTKA FTGLAILKLA QEGRLNLNDA
     VSKHVPHFKM NYNGQNETIT IKQLLAQTSG IPSDITSEDA VTNKNNRLND VTRAIMGDEL
     HHKPGEEFEY SNMNYDLLGL IIQNVTKQSY TQYITDHWLK PLQMKHTTFK QTNYKSKHDA
     IGYELQGSTP VVSKPEFNLW DTPSAYMMTS TEDLEHWIKF QLNPPDKYKS LVQQSHKNLS
     STIGEPNANP YASGWFTNND EHLVFHSGTL DNFSSFILLN PKQNYGIVVL ANLNSEYVPK
     LVEHLNTQIV NHKRYSTVAS ILNQYKDQFN IVTVLMTTLI LLAFIFSAYR AWQMRHGQIL
     LRRSKRIAVL SWLTLCLCIA IALILYALPY LILGSNNWSF VLTWLPIEIK LALITTLIAL
     FSTLIVILLF LHTKITKT