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Database: UniProt
Entry: A0A0A7FZH4_9CLOT
LinkDB: A0A0A7FZH4_9CLOT
Original site: A0A0A7FZH4_9CLOT 
ID   A0A0A7FZH4_9CLOT        Unreviewed;       286 AA.
AC   A0A0A7FZH4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase family protein {ECO:0000313|EMBL:AIY84246.1};
GN   ORFNames=U729_2449 {ECO:0000313|EMBL:AIY84246.1};
OS   Clostridium baratii str. Sullivan.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY84246.1, ECO:0000313|Proteomes:UP000030635};
RN   [1] {ECO:0000313|EMBL:AIY84246.1, ECO:0000313|Proteomes:UP000030635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sullivan {ECO:0000313|EMBL:AIY84246.1};
RX   PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA   Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA   Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA   Karavis M.A., Smith L.A.;
RT   "Genomic sequences of six botulinum neurotoxin-producing strains
RT   representing three clostridial species illustrate the mobility and
RT   diversity of botulinum neurotoxin genes.";
RL   Infect. Genet. Evol. 30:102-113(2014).
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DR   EMBL; CP006905; AIY84246.1; -; Genomic_DNA.
DR   RefSeq; WP_039315422.1; NZ_CP006905.1.
DR   AlphaFoldDB; A0A0A7FZH4; -.
DR   STRING; 1561.NPD11_589; -.
DR   KEGG; cbv:U729_2449; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_3_1_9; -.
DR   OrthoDB; 43070at2; -.
DR   Proteomes; UP000030635; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404:SF5; AUTOLYSIN PH-RELATED; 1.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030635};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          163..282
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          33..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   286 AA;  31879 MW;  6734A22E948AE8C7 CRC64;
     MKKIIIFIIA LIFSTSLIYY IVNSNKSNEK INENETTVST KNSSNKTNLK DELKKLEKNV
     EKNNEKKSDK NSNKDNKKKD ITIVIDPGHS NKATTETEPI SPNSKEKKLK DTLGSTGVNS
     KVPEYVITNG VALSLEKILK NDGYNVIMTK RDINTPMTNI ERTEIGNKNK ANLMIRIHCD
     GVDSQSAVGA SMLVPEAKGN VTPKISKESK EYGEKIINKY TSYLGLKNRG IVYRDDLTGF
     NWSKVPIVLI ELGFISNPKE DALLSNKENY NKIATGIANG INDCFK
//
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