ID D6XYQ4_BACIE Unreviewed; 759 AA.
AC D6XYQ4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Transglutaminase domain protein {ECO:0000313|EMBL:ADH98212.1};
GN OrderedLocusNames=Bsel_0677 {ECO:0000313|EMBL:ADH98212.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98212.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH98212.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001791; ADH98212.1; -; Genomic_DNA.
DR RefSeq; WP_013171641.1; NC_014219.1.
DR AlphaFoldDB; D6XYQ4; -.
DR STRING; 439292.Bsel_0677; -.
DR KEGG; bse:Bsel_0677; -.
DR eggNOG; COG1305; Bacteria.
DR HOGENOM; CLU_021791_1_0_9; -.
DR OMA; YYKNAFI; -.
DR OrthoDB; 9804872at2; -.
DR Proteomes; UP000000271; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.10.620.30; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025403; TgpA-like_C.
DR InterPro; IPR021878; TgpA_N.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR42736; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR PANTHER; PTHR42736:SF1; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR Pfam; PF13559; DUF4129; 1.
DR Pfam; PF11992; TgpA_N; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 495..570
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 589..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..603
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 86290 MW; 9C5AEE1DDBF93E57 CRC64;
MKQKQKRSFS VVHLFIYVLA FLILWEWLRP IPAVTDTSSI EVFLLFAAVS AALIYIRLPF
WVNIPTLAVF AVFGLHRIFY EGPFFSREGG GESVRLIGGE IRHNAALLIS GDMELLTNPF
RTLLLFLLLA LICYLMYFWV FQTRRVFFFL LATVVYITIL DTFTVVDASQ AIVRIVVIGF
FMMTLLHMLA VQEEEKNIGR ESEPVLPAAW MYTLTAMVTV ALAAGFLLPK PDPQWSDPVP
AMRSFLTGEG GIGGGGGTIR RVGYGDNDER LGGGFVEDES VVFEAVVDGP VYWRGESKDE
YTGLGWVNSE TDFQPATDVF DPDRIDYWMY DEDLTSGEDW LEADVEMVTE ADFPLFFYAG
QPMDIPGESV GASVDVTPQT AFVDPLTGRI EATEPGQGER IDSYTFSYKD FSFPIPTMQE
TEENDPQALF ERYTQLPDDL PERVIDLAFE ITEEEDNRYD KAVAVEQYFG QNDFVYQTTD
VPVPEEGQDY VDQFLFETQA GYCDNYSTSM VVLLRALDIP ARWVKGFTSG EQTEVLDDGR
SVYEVSNTNA HSWVEVYFPE VGWVPFEPTQ GFENYADFQT EPIEIDLDLD GEDAEDPDDP
ERPDTPDSEF PDPDEGFDPG EAVGDGGDGT GAAPFRDFLT PGNILISLVV LFFVLFAYQK
QSKLMNRFFF LIYKLKGTDR SFLKAYRRLL WLLEKEGLPR GEGETLREYA RRADQAFSSQ
AMSKLTKAYE RIYYGGFDPD GDWQKHRKDW EEMLKRLYQ
//