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Database: UniProt
Entry: R7G921_9FIRM
LinkDB: R7G921_9FIRM
Original site: R7G921_9FIRM 
ID   R7G921_9FIRM            Unreviewed;       436 AA.
AC   R7G921;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Putative delta-lactam-biosynthetic de-N-acetylase {ECO:0000313|EMBL:CDE22497.1};
GN   ORFNames=BN631_01010 {ECO:0000313|EMBL:CDE22497.1};
OS   Amedibacillus dolichus CAG:375.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Amedibacillus.
OX   NCBI_TaxID=1263076 {ECO:0000313|EMBL:CDE22497.1, ECO:0000313|Proteomes:UP000018093};
RN   [1] {ECO:0000313|EMBL:CDE22497.1, ECO:0000313|Proteomes:UP000018093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:375 {ECO:0000313|Proteomes:UP000018093};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDE22497.1}.
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DR   EMBL; CBIN010000087; CDE22497.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7G921; -.
DR   Proteomes; UP000018093; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR032179; Cry22Aa_Ig-like.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10587:SF78; PEPTIDOGLYCAN-N-ACETYLMURAMIC ACID DEACETYLASE PDAA; 1.
DR   Pfam; PF16403; Bact_surface_Ig-like; 2.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018093};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          240..424
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   436 AA;  50625 MW;  0C0924604C616B00 CRC64;
     MSKRCKIIVN SIIVFVLLLI VGIIVKFVFF SGSFTPLLKL NGDKQMVIDV HQEFEDPFVK
     ARYHLKDISD EVEVLGQVDC EKIGTYQLVY RLKEHDKEVV REVKVVDRTA PKLMLKGASH
     VRVFLGGKYQ ESGYAASDDV DGDLSDEVRV ESHVNMNKKG IYKIHYYVKD HSGNGSKRTR
     SVEVCEDPTS LKLHYNYDTY DNTMEEWWFH KSEKHERNKG AKSAAYLKKF DTYYQGPDEK
     VIYLTFDEGG NEVTYSKEIA EILKKHDVQA TYFFTLNYLR DEADFVKELV ANGNLIGNHT
     WHHYDMTTLA NAHSVDKFVK EITETEKMYM EITGEEMPKI FRFPRGGGSE RTMKMVQDLG
     YRNYYWSHAF YDYGDDVSKE EALRTMMEHY HNGAIYLLHP SNRGNYEAIE SFIVAMKDLG
     YRFETLDAIG KDSQEP
//
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