ID   Y130_LISMO              Reviewed;         784 AA.
AC   Q8YAJ5;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cell wall protein Lmo0130 {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=lmo0130;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 156-165; 181-195 AND 349-364, PROCESSING BY SRTA, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11929538; DOI=10.1046/j.1365-2958.2002.02798.x;
RA   Bierne H., Mazmanian S.K., Trost M., Pucciarelli M.G., Liu G., Dehoux P.,
RA   Jansch L., Garcia-del Portillo F., Schneewind O., Cossart P.;
RT   "Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring
RT   of surface proteins and affects virulence.";
RL   Mol. Microbiol. 43:869-881(2002).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND PROCESSING BY SRTA.
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=16247833; DOI=10.1002/pmic.200402075;
RA   Pucciarelli M.G., Calvo E., Sabet C., Bierne H., Cossart P.,
RA   Garcia-del Portillo F.;
RT   "Identification of substrates of the Listeria monocytogenes sortases A and
RT   B by a non-gel proteomic analysis.";
RL   Proteomics 5:4808-4817(2005).
RN   [4]
RP   SUBCELLULAR LOCATION, AND PROCESSING BY SRTA.
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=22837151; DOI=10.2436/20.1501.01.157;
RA   Mariscotti J.F., Quereda J.J., Pucciarelli M.G.;
RT   "Contribution of sortase A to the regulation of Listeria monocytogenes
RT   LPXTG surface proteins.";
RL   Int. Microbiol. 15:43-51(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477, ECO:0000269|PubMed:11929538,
CC       ECO:0000269|PubMed:16247833, ECO:0000269|PubMed:22837151};
CC       Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477,
CC       ECO:0000269|PubMed:11929538, ECO:0000269|PubMed:16247833}. Note=In the
CC       absence of SrtA in exponential phase some protein is still anchored to
CC       the cell wall while a very small amount is secreted, in stationary
CC       phase almost no protein accumulates; protein levels decrease in the
CC       srtA mutant, suggesting post-transcriptional regulation that involves
CC       SrtA. {ECO:0000269|PubMed:22837151}.
CC   -!- INDUCTION: Present in both exponential and stationary phase (at protein
CC       level). {ECO:0000269|PubMed:16247833}.
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DR   EMBL; AL591973; CAC98345.1; -; Genomic_DNA.
DR   PIR; AC1091; AC1091.
DR   RefSeq; NP_463663.1; NC_003210.1.
DR   RefSeq; WP_010989350.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8YAJ5; -.
DR   SMR; Q8YAJ5; -.
DR   STRING; 169963.lmo0130; -.
DR   PaxDb; Q8YAJ5; -.
DR   EnsemblBacteria; CAC98345; CAC98345; CAC98345.
DR   GeneID; 986721; -.
DR   KEGG; lmo:lmo0130; -.
DR   PATRIC; fig|169963.11.peg.133; -.
DR   eggNOG; COG0737; Bacteria.
DR   HOGENOM; CLU_005854_5_1_9; -.
DR   OMA; VQPFTNM; -.
DR   PhylomeDB; Q8YAJ5; -.
DR   BioCyc; LMON169963:LMO0130-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008768; F:UDP-sugar diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0009166; P:nucleotide catabolic process; IBA:GO_Central.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; -; 1.
DR   InterPro; IPR008334; 5'-Nucleotdase_C.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006146; 5'-Nucleotdase_CS.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR041498; Big_6.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR11575; PTHR11575; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF17936; Big_6; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; SSF55816; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Direct protein sequencing; Peptidoglycan-anchor;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..784
FT                   /note="Cell wall protein Lmo0130"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004316651"
FT   PROPEP          759..784
FT                   /note="Removed by sortase A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT                   ECO:0000269|PubMed:11929538, ECO:0000305|PubMed:16247833,
FT                   ECO:0000305|PubMed:22837151"
FT                   /id="PRO_0000445902"
FT   REGION          690..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           755..759
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   MOD_RES         758
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT                   ECO:0000305|PubMed:11929538"
SQ   SEQUENCE   784 AA;  82510 MW;  99686C2FF07AE133 CRC64;
     MKVNKFFKKT THVLLVAGLT IGLTAPFTGT TAQAAADTVP IQILGINDFH GALETASKDA
     SGSPIGGADY LATNLDNATN SFLQANPGAT TDNAIRVQAG DMVGASPAVS GLLQDEPTMK
     VLQKMNFEVG TLGNHEFDEG LPEYKRILDG VSTNKFGPIV EAYPRVKSDM KIVAANVVNK
     GTNTVAEGFL PYYVKEIDGV KVGFIGIVTT EIPNLVLANH IKDYDFLDEA ETIVKYSAEL
     RGQGVNAIVV LSHVPALSTG NPNTGTKQDV AGEAANMMTK ANELDPNNSV DLVLAGHNHQ
     YTNGLVGKTR IVQSYNNGKA FSDVTGELDK TTGDFVSPPD AKITYNTRSV TPNADITAVT
     EDAKSRIEGV INETIGLANK DVISRDTNPD NKAIDDKESE LGNMITDAQR YMANKAGADV
     DFAMTNNGGI RSDLTTRLAN GQNEITWGAA QAVQPFGNIL QVVEMTGADI LEALNQQYLS
     NQTYFLQISG LKYTFTDTDD LDHAYKVASV TTEDGTPLKT DQKYKVVIND FLFGGGDGFS
     AFKKANLVTA IDPDTETFIN YIKDQKAAGK VITAQKEGRK VYKSQAEIDK ETKDAAIKAI
     KEATKINKLA EKDKTLTGTT LPGATVSVQK ATANARMALA AGPNATADAN GKFSVDVTSL
     NLKKGDQITT TITDPNGYST TFQATVQAAA TTPPDNGNGG TDNGNGNGNN GGTDGNGGTN
     NGNGSGTNGG TTTTEDPTTT TSNTSTTGTS SNTSLPTTGD TAGLATVFGV ILTTTALYVL
     RKRS