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Database: UniProt
Entry: C1FQ38_CLOBJ
LinkDB: C1FQ38_CLOBJ
Original site: C1FQ38_CLOBJ 
ID   C1FQ38_CLOBJ            Unreviewed;       352 AA.
AC   C1FQ38;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=3D/G5 domain protein {ECO:0000313|EMBL:ACO85930.1};
GN   OrderedLocusNames=CLM_0122 {ECO:0000313|EMBL:ACO85930.1};
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232 {ECO:0000313|EMBL:ACO85930.1, ECO:0000313|Proteomes:UP000001374};
RN   [1] {ECO:0000313|EMBL:ACO85930.1, ECO:0000313|Proteomes:UP000001374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2 {ECO:0000313|Proteomes:UP000001374};
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001581; ACO85930.1; -; Genomic_DNA.
DR   RefSeq; WP_012705025.1; NC_012563.1.
DR   AlphaFoldDB; C1FQ38; -.
DR   KEGG; cby:CLM_0122; -.
DR   eggNOG; COG3583; Bacteria.
DR   eggNOG; COG3584; Bacteria.
DR   HOGENOM; CLU_036884_0_1_9; -.
DR   Proteomes; UP000001374; Chromosome.
DR   GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro.
DR   CDD; cd22786; DPBB_YuiC-like; 1.
DR   Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR007137; DUF348.
DR   InterPro; IPR011098; G5_dom.
DR   InterPro; IPR026044; MltA.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR30124; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR   PANTHER; PTHR30124:SF0; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF03990; DUF348; 2.
DR   Pfam; PF07501; G5; 1.
DR   SMART; SM01208; G5; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   PROSITE; PS51109; G5; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          150..230
FT                   /note="G5"
FT                   /evidence="ECO:0000259|PROSITE:PS51109"
SQ   SEQUENCE   352 AA;  38386 MW;  309245B6D98D97B8 CRC64;
     MVEKLKKKIK EHFSNGPKAI LIVVVILMIA SIVITNMRKT IIVSIDGKES QKITTFKKTY
     AKALTSKNIQ VGPKDKVQPQ LDAEIKDGSK LSIKKAVKVN VEVDGKKLAI QSAEDNIGDM
     LKKEGIQVKK LDKVAPSKEE EIRKGLKVTV TRVEEKVIKS KKNMDYETVV KEDDSLEKGD
     KKVIREGQNG EKEVTTKVVF EDGKEKVRKV VSESIKKQPV SKVVAMGTKV TTVNALSRGG
     SVTGTPGGRS LRMRATAYTS SYEDTGKSPG SPDFGVTATG TTARRNSGGY SSIAVDPRVI
     PLGTKLFVEG YGYAIAEDTG GAIKGNVIDL YFDSNVEVSN WGSRWVNVYI LD
//
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