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Database: UniProt
Entry: A0A074LM63_9BACL
LinkDB: A0A074LM63_9BACL
Original site: A0A074LM63_9BACL 
ID   A0A074LM63_9BACL        Unreviewed;       742 AA.
AC   A0A074LM63;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=PASTA domain-containing protein {ECO:0000259|PROSITE:PS51178};
GN   ORFNames=EL26_10855 {ECO:0000313|EMBL:KEO83186.1};
OS   Tumebacillus flagellatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO83186.1, ECO:0000313|Proteomes:UP000027931};
RN   [1] {ECO:0000313|EMBL:KEO83186.1, ECO:0000313|Proteomes:UP000027931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GST4 {ECO:0000313|EMBL:KEO83186.1,
RC   ECO:0000313|Proteomes:UP000027931};
RX   PubMed=23435245; DOI=10.1099/ijs.0.045351-0;
RA   Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.;
RT   "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase-producing
RT   bacterium isolated from cassava wastewater.";
RL   Int. J. Syst. Evol. Microbiol. 63:3138-3142(2013).
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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:KEO83186.1}.
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DR   EMBL; JMIR01000013; KEO83186.1; -; Genomic_DNA.
DR   RefSeq; WP_052036227.1; NZ_JMIR01000013.1.
DR   AlphaFoldDB; A0A074LM63; -.
DR   STRING; 1157490.EL26_10855; -.
DR   eggNOG; COG0768; Bacteria.
DR   OrthoDB; 2378949at2; -.
DR   Proteomes; UP000027931; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   CDD; cd06575; PASTA_Pbp2x-like_2; 1.
DR   Gene3D; 3.30.10.20; -; 1.
DR   Gene3D; 3.30.450.330; -; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR   Pfam; PF03793; PASTA; 2.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00740; PASTA; 2.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR   SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2.
DR   PROSITE; PS51178; PASTA; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027931};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        14..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          614..677
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          681..740
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          590..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  81163 MW;  23993D5D2B9B094C CRC64;
     MKEQERTFRK RSKLLRFGLL VGMSSLVLRL FYVQVAEANS LSEKAQDWIK TEKDIVGTRG
     AIFDRNGQKL AFTGVAYDIN VDVSFFRKDK AKEKGDTPEE YAKFLAPLLG MTESDVLGYI
     NLTDPKIQGV GLGPKGKKVD SSIADKIEAA HKDKKFLGIT ANRTDIRRYP SGSLAAHVLG
     FYGMNPADGK DTGLAGVESV YDKELTGDPG HMEYFTDRDG YPLPNYEPKV TKQPTDGKDV
     VLTIDETIQH FVEDELDNIV NKYAPKHATI IVADPNNGEI LALGNRPTFK PAEYASADKE
     ALWNDFALRS FEPGSTFKTF VLTGALAENK LDLSEKFQSG SITVDGMTVR DWNGVGFGDI
     SYREAVYNSS NVGFVKIGQK LGKDDLFKYL YDFGFNKPTG IDLPGEENAS LFDPKKMSDI
     DLASTSFGQG VSVTPMQQIA AMMAVCNGGK VYQPHVVKEL RDQKTGATVE EIKPKVTHEV
     ANPEVFQTVR QVLEETVLAD ANKTDYIRGY HVAGKTGTAQ VPKENGVGYD DDHYRLSFTG
     FAPANNPRLL IYVDVDQPSR NAPLQFGSIE AAPSGKVVLE EALHYLQVPI DPNDNTVPQT
     DSKTGESPKV AKPAEPKTFV NVPDLIGTTK DQAVELTKQN GLKIQEVGDG PKATGQWPDV
     TYGQVPAGTE VKVYFGPEGT KDGKVKMPDL RGLSMREAME TLSLLQLQME PNGSGYVIKQ
     GVAPGTMVPF GSSVKLDFAP QS
//
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