ID   AMIA_SALTY              Reviewed;         289 AA.
AC   P33772;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase AmiA;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=amiA; OrderedLocusNames=STM2450;
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 [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=8349542; DOI=10.1128/jb.175.16.4990-4999.1993;
RA   Xu K., Elliott T.;
RT   "An oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of
RT   Salmonella typhimurium.";
RL   J. Bacteriol. 175:4990-4999(1993).
RN   [2]
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).
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   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; L19503; AAA27138.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21344.1; -; Genomic_DNA.
DR   PIR; A53302; A53302.
DR   RefSeq; NP_461385.1; NC_003197.2.
DR   RefSeq; WP_000102881.1; NC_003197.2.
DR   AlphaFoldDB; P33772; -.
DR   SMR; P33772; -.
DR   STRING; 99287.STM2450; -.
DR   PaxDb; P33772; -.
DR   EnsemblBacteria; AAL21344; AAL21344; STM2450.
DR   GeneID; 1253972; -.
DR   KEGG; stm:STM2450; -.
DR   PATRIC; fig|99287.12.peg.2588; -.
DR   HOGENOM; CLU_014322_4_1_6; -.
DR   OMA; QIRPVHH; -.
DR   PhylomeDB; P33772; -.
DR   BioCyc; SENT99287:STM2450-MON; -.
DR   PHI-base; PHI:8728; -.
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..34
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..289
FT                   /note="N-acetylmuramoyl-L-alanine amidase AmiA"
FT                   /id="PRO_0000006461"
FT   DOMAIN          59..273
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
FT   REGION          36..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   289 AA;  31659 MW;  8FCC21089D56F671 CRC64;
     MSTFKLLKTL TSRRQVLKTG LAALTLSGMS HAVAKEETLK TSNGHSKPKT KKTGSKRLVM
     LDPGHGGIDT GAIGRNGSQE KHVVLAIAKN VRAILRNHGI DARLTRTGDT FIPLYDRVEI
     AHKHGADLFM SIHADGFTNP KAAGASVFAL SNRGASSAMA KYLSERENRA DEVAGKKATD
     RDHLLQQVLF DLVQTDTIKN SLTLGSHILK KIKPIHKLHS RTTEQAAFVV LKSPSIPSVL
     VETSFITNPE EERLLGTTAF RQKIATAIAN GIISYFHWFD NQKAHTKKR