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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//