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Database: UniProt
Entry: A8F9C6_BACP2
LinkDB: A8F9C6_BACP2
Original site: A8F9C6_BACP2 
ID   A8F9C6_BACP2            Unreviewed;       237 AA.
AC   A8F9C6;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ABV60843.1};
GN   OrderedLocusNames=BPUM_0144 {ECO:0000313|EMBL:ABV60843.1};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV60843.1, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ABV60843.1, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV60843.1,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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DR   EMBL; CP000813; ABV60843.1; -; Genomic_DNA.
DR   RefSeq; WP_012008723.1; NZ_VEIS01000020.1.
DR   AlphaFoldDB; A8F9C6; -.
DR   STRING; 315750.BPUM_0144; -.
DR   KEGG; bpu:BPUM_0144; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_7_0_9; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000001355; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR014234; Spore_CwlD.
DR   NCBIfam; TIGR02883; spore_cwlD; 1.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          115..226
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   237 AA;  26990 MW;  B612A50AD297EEA6 CRC64;
     MKRKLKWTGF LIGFIVLLFL FRFQFLNDDS WKSWNLPLSG KIIYLDPGHG GPDGGAVGGE
     LLEKEIALDV SMKIRDYLQE QGALVLMTRE DDSDLSSKNT KGYARKKAED LRNRVKAINE
     SEADFYLSIH LNAIPSNKWS GAQTFFYGKY EENEKAAKFI QDELRNNLEN TDRKAKRING
     IYLMQNVTKP GALVEIGFLS NPKEASQLAT PKYQDQIAAS IYKGILRYLT EQKEPPE
//
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