ID C2CF81_9FIRM Unreviewed; 259 AA.
AC C2CF81;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Peptidase C26 {ECO:0000313|EMBL:EEI83700.1};
GN ORFNames=HMPREF0077_0141 {ECO:0000313|EMBL:EEI83700.1};
OS Anaerococcus tetradius ATCC 35098.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525255 {ECO:0000313|EMBL:EEI83700.1, ECO:0000313|Proteomes:UP000003744};
RN [1] {ECO:0000313|EMBL:EEI83700.1, ECO:0000313|Proteomes:UP000003744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35098 {ECO:0000313|EMBL:EEI83700.1,
RC ECO:0000313|Proteomes:UP000003744};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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:EEI83700.1}.
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DR EMBL; ACGC01000009; EEI83700.1; -; Genomic_DNA.
DR RefSeq; WP_004835833.1; NZ_GG666295.1.
DR AlphaFoldDB; C2CF81; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_2_0_9; -.
DR Proteomes; UP000003744; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01745; GATase1_2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR011697; Peptidase_C26.
DR InterPro; IPR044668; PuuD-like.
DR PANTHER; PTHR43235; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR PANTHER; PTHR43235:SF1; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR Pfam; PF07722; Peptidase_C26; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 130
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 234
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 259 AA; 29502 MW; D24290545BBB5872 CRC64;
MISKFFKFIK ISLFLILVVL AFIMIRDNFF PHKIIGIVHN NQNINDIKIA TGDNRAIVND
IDTSRMDLDM CKRKIDSCDG VIFAGGNDFD PDLYGGDRSL VETYSREDDD KSLSILDYCI
GLQKPILGIC RGMQLINIYY GGSLYDDIAK QFSDKICHRN KDNTLAYHDI SISPDTRLMK
IAKSDRLEVN SYHHEGIKDL GDGLTVSARS DDGLIEAIEN PYYPYMIGVQ WHPEINYEEN
DLSKRLLKDF IKNSNAGKN
//
