ID   AMIC_NEIMB              Reviewed;         416 AA.
AC   Q9K0V3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase AmiC;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=amiC; OrderedLocusNames=NMB0456;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17038831; DOI=10.4161/hv.1.2.1651;
RA   Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.;
RT   "Characterization of the protein content of a meningococcal outer membrane
RT   vesicle vaccine by polyacrylamide gel electrophoresis and mass
RT   spectrometry.";
RL   Hum. Vaccin. 1:80-84(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=NZ98/254 / Serogroup B;
RX   PubMed=16645985; DOI=10.1002/pmic.200500821;
RA   Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT   "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT   prepared from the group B strain NZ98/254.";
RL   Proteomics 6:3400-3413(2006).
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   -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC       used as vaccines in human.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; AE002098; AAF40893.1; -; Genomic_DNA.
DR   PIR; B81198; B81198.
DR   RefSeq; NP_273503.1; NC_003112.2.
DR   RefSeq; WP_002224939.1; NC_003112.2.
DR   AlphaFoldDB; Q9K0V3; -.
DR   SMR; Q9K0V3; -.
DR   STRING; 122586.NMB0456; -.
DR   PaxDb; Q9K0V3; -.
DR   DNASU; 902572; -.
DR   EnsemblBacteria; AAF40893; AAF40893; NMB0456.
DR   KEGG; nme:NMB0456; -.
DR   PATRIC; fig|122586.8.peg.579; -.
DR   HOGENOM; CLU_014322_2_2_4; -.
DR   OMA; KRYFAAN; -.
DR   Proteomes; UP000000425; 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; IPR021731; AMIN_dom.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF11741; AMIN; 1.
DR   SMART; SM00646; Ami_3; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Hydrolase; Periplasm; Reference proteome;
KW   Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..416
FT                   /note="N-acetylmuramoyl-L-alanine amidase AmiC"
FT                   /id="PRO_0000320265"
FT   DOMAIN          192..405
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
FT   REGION          166..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  45190 MW;  5E89E0A60DE8AD21 CRC64;
     MIKLTRRQII RRTAGTLFAL SPIASAVAKT VRAPQFTAAR IWPSHTYTRL TLESTAALKY
     QHFTLDNPGR LVVDIQNANI NTVLHGLSQK VMADDPFIRS IRAGQNTPTT VRLVIDLKQP
     THAQVFALPP VGGFKNRLVV DLYPHGMDAD DPMMALLNGS LNKTLRGSPE ADLAQNTTPQ
     PGRGRNGRRP VIMLDPGHGG EDPGAISPGG LQEKHVVLSI ARETKNQLEA LGYNVFMTRN
     EDVFIPLGVR VAKGRARRAD VFVSIHADAF TSPSARGTGV YMLNTKGATS SAAKFLEQTQ
     NNADAVGGVP TSGNRNVDTA LLDMTQTATL RDSRKLGKLV LEELGRLNHL HKGRVDEANF
     AVLRAPDMPS ILVETAFLSN PAEEKLLGSE SFRRQCAQSI ASGVQRYINT SVLKRG