ID   AMIB_SALTY              Reviewed;         439 AA.
AC   P26366;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase AmiB;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=amiB; OrderedLocusNames=STM4358;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 340-439.
RC   STRAIN=LT2;
RX   PubMed=2676972; DOI=10.1128/jb.171.10.5325-5331.1989;
RA   Mankovich J.A., McIntyre C.A., Walker G.C.;
RT   "Nucleotide sequence of the Salmonella typhimurium mutL gene required for
RT   mismatch repair: homology of MutL to HexB of Streptococcus pneumoniae and
RT   to PMS1 of the yeast Saccharomyces cerevisiae.";
RL   J. Bacteriol. 171:5325-5331(1989).
CC   -!- FUNCTION: Cell-wall hydrolase involved in septum cleavage during cell
CC       division. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; AE006468; AAL23178.1; -; Genomic_DNA.
DR   EMBL; M29687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_463219.1; NC_003197.2.
DR   RefSeq; WP_000640362.1; NC_003197.2.
DR   AlphaFoldDB; P26366; -.
DR   SMR; P26366; -.
DR   STRING; 99287.STM4358; -.
DR   PaxDb; P26366; -.
DR   EnsemblBacteria; AAL23178; AAL23178; STM4358.
DR   GeneID; 1255884; -.
DR   KEGG; stm:STM4358; -.
DR   PATRIC; fig|99287.12.peg.4582; -.
DR   HOGENOM; CLU_014322_2_3_6; -.
DR   OMA; NADPMFK; -.
DR   PhylomeDB; P26366; -.
DR   BioCyc; SENT99287:STM4358-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Periplasm; Reference proteome;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..439
FT                   /note="N-acetylmuramoyl-L-alanine amidase AmiB"
FT                   /id="PRO_0000006463"
FT   DOMAIN          188..407
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
FT   REGION          138..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  46790 MW;  01B2BEB753D34DE9 CRC64;
     MIYRIKNAVI AALILLCAQA GAASLSDIQV SNGEQQARIT LSFIGEPEYA YSQDGKRTVA
     LDIRQTGVIQ GLPLQFSGNN LVKTIRAGTP KDAQSLRLLV DLTENGKTEA VKRQNGGNYT
     VIFTINADVP PPPPPVVAKR VESAPRPTEP ARNPFKSSDD RLTGVTSSNT VTRPAARASA
     GAGDKVVIAI DAGHGGQDPG AIGPGGTREK NVTIAIARKL RTLLNNDPMF KGVLTRDGDY
     FISVMGRSDV ARKQNANFLV SIHADAAPNR DATGASVWVL SNRRANSEMA NWLEQHEKQS
     ELLGGAGDVL ANSQSDPYLS QAVLDLQFGH SQRVGYDVAT NVLSQLDGVG SLHKRRPEHA
     SLGVLRSPDI PSILVETGFI SNHGEERLLA SDRYQQQIAD AIYRGLRKYF AAHPIQSAPQ
     GGPGQTASTN QPGAITAAN