ID   AMIB_HAEIN              Reviewed;         432 AA.
AC   P44493;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Probable N-acetylmuramoyl-L-alanine amidase AmiB;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=amiB; OrderedLocusNames=HI_0066;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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   -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC       binding.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC21744.1; -; Genomic_DNA.
DR   PIR; D64046; D64046.
DR   RefSeq; NP_438239.1; NC_000907.1.
DR   RefSeq; WP_005693856.1; NC_000907.1.
DR   AlphaFoldDB; P44493; -.
DR   SMR; P44493; -.
DR   STRING; 71421.HI_0066; -.
DR   EnsemblBacteria; AAC21744; AAC21744; HI_0066.
DR   KEGG; hin:HI_0066; -.
DR   PATRIC; fig|71421.8.peg.67; -.
DR   eggNOG; COG0860; Bacteria.
DR   eggNOG; COG1388; Bacteria.
DR   HOGENOM; CLU_014322_2_4_6; -.
DR   OMA; TRKSDYY; -.
DR   PhylomeDB; P44493; -.
DR   BioCyc; HINF71421:G1GJ1-67-MON; -.
DR   Proteomes; UP000000579; 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; cd00118; LysM; 2.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.10.350.10; -; 2.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF01476; LysM; 2.
DR   SMART; SM00646; Ami_3; 1.
DR   SMART; SM00257; LysM; 2.
DR   SUPFAM; SSF54106; SSF54106; 2.
DR   PROSITE; PS51782; LYSM; 2.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Periplasm; Reference proteome;
KW   Repeat; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..432
FT                   /note="Probable N-acetylmuramoyl-L-alanine amidase AmiB"
FT                   /id="PRO_0000006464"
FT   DOMAIN          25..244
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          292..335
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          385..429
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
SQ   SEQUENCE   432 AA;  49109 MW;  008D918A0E1EE81D CRC64;
     MKTKILFFLF FSTFSFSIFA APITIAIDPG HGGKDPGAIS RNLGIYEKNV TLSIAKELKA
     LLDKDPHFRG VLTRKSDYYI SVPERSEIAR KFKANYLISI HADSSKSPDR RGASVWVLSN
     RRANDEMGQW LEDDEKRSEL LGGAGKVLSH NNDKYLDQTV LDLQFGHSQR TGYVLGEHIL
     HHFAKVTTLS RSTPQHASLG VLRSPDIPSV LVETGFLSNS EEEKKLNSQT YRRRIAYMIY
     EGLVAFHSGK TNTLVKDNLV QNIKQNDIKK SGKNNRTSEQ NINEDNIKDS GIRHIVKKGE
     SLGSLSNKYH VKVSDIIKLN QLKRKTLWLN ESIKIPDNVE IKNKSLTIKE NDFHKKQNSL
     VNNTNKDLKK EKNTQTNNQK NIIPLYHKVT KNQTLYAISR EYNIPVNILL SLNPHLKNGK
     VITGQKIKLR EK