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Database: UniProt
Entry: B6BNW6_SULGG
LinkDB: B6BNW6_SULGG
Original site: B6BNW6_SULGG 
ID   B6BNW6_SULGG            Unreviewed;       466 AA.
AC   B6BNW6; H1FUR3;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EHP28920.1};
DE            EC=3.5.1.28 {ECO:0000313|EMBL:EHP28920.1};
GN   Name=amiC {ECO:0000313|EMBL:EHP28920.1};
GN   ORFNames=SMGD1_0393 {ECO:0000313|EMBL:EHP28920.1};
OS   Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP28920.1, ECO:0000313|Proteomes:UP000006431};
RN   [1] {ECO:0000313|EMBL:EHP28920.1, ECO:0000313|Proteomes:UP000006431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD1 {ECO:0000313|EMBL:EHP28920.1,
RC   ECO:0000313|Proteomes:UP000006431};
RX   PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA   Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA   Labrenz M., Jurgens K.;
RT   "Genome and physiology of a model Epsilonproteobacterium responsible for
RT   sulfide detoxification in marine oxygen depletion zones.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
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:EHP28920.1}.
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DR   EMBL; AFRZ01000001; EHP28920.1; -; Genomic_DNA.
DR   RefSeq; WP_008340087.1; NZ_DS995293.1.
DR   AlphaFoldDB; B6BNW6; -.
DR   STRING; 929558.SMGD1_0393; -.
DR   PATRIC; fig|929558.5.peg.391; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_11_1_7; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000006431; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 2.60.40.3500; -; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EHP28920.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006431};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..466
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002843211"
FT   DOMAIN          306..460
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   466 AA;  53261 MW;  036AE978793E504B CRC64;
     MVRLLSLLLI LAISIYAQSD SEILKRADGF MKSTSKSNHF RAYNDYKNLY LRAIMSEDSK
     LRINSLKGIV KSGNKLHIDV SQYSDELSKI KPKTSYQTPV PKPMKTSSQA KNIKLQSSHK
     LKSVRWKDDK LILKFDNKLR SNQINYFTLY DSKNERYRYI FDIQASMLTE SQTLRKNDID
     RIELAQYNTN TLRLVVENSQ KVEISFKKDS NQLVVHMLSK SSDKYSKAFK TIVKSTIPLR
     ADRNKTIVID AGHGGKDPGA VGYRNYREKV VVFKIAQELK NILKSRGYKV YMTRDRDKFV
     KLSNRTEYAN IKKADIFVSI HANAVGRKNA NKAQGVECYF LSPSRSERAE KVAAKENSAD
     LSDMNRYGKD TFLNFLNSHK IVASNKLAID LQRGMLGSVN KNYRVRDGGV REGPFWVLVG
     AQMPAVLVEV GFISHPEEAK RLVDDKYRKT MALGLANGIE RYFAKN
//
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