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Database: UniProt
Entry: A0A5C8P0F8_9BACI
LinkDB: A0A5C8P0F8_9BACI
Original site: A0A5C8P0F8_9BACI 
ID   A0A5C8P0F8_9BACI        Unreviewed;      1924 AA.
AC   A0A5C8P0F8;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   02-APR-2025, entry version 24.
DE   SubName: Full=LPXTG cell wall anchor domain-containing protein {ECO:0000313|EMBL:TXL66715.1};
GN   ORFNames=FHP05_04850 {ECO:0000313|EMBL:TXL66715.1};
OS   Cerasibacillus terrae.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Cerasibacillus.
OX   NCBI_TaxID=2498845 {ECO:0000313|EMBL:TXL66715.1, ECO:0000313|Proteomes:UP000321574};
RN   [1] {ECO:0000313|EMBL:TXL66715.1, ECO:0000313|Proteomes:UP000321574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-CFT480 {ECO:0000313|EMBL:TXL66715.1,
RC   ECO:0000313|Proteomes:UP000321574};
RA   Lin S.-Y., Tsai C.-F., Young C.-C.;
RT   "Cerasibacillus sp. nov., isolated from maize field.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000256|ARBA:ARBA00004168}; Peptidoglycan-anchor
CC       {ECO:0000256|ARBA:ARBA00004168}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TXL66715.1}.
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DR   EMBL; VDUW01000002; TXL66715.1; -; Genomic_DNA.
DR   RefSeq; WP_147666114.1; NZ_VDUW01000002.1.
DR   OrthoDB; 9772095at2; -.
DR   Proteomes; UP000321574; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 2.60.40.1260; Lamin Tail domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR001322; Lamin_tail_dom.
DR   InterPro; IPR036415; Lamin_tail_dom_sf.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR051918; STPP_CPPED1.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   PANTHER; PTHR43143; METALLOPHOSPHOESTERASE, CALCINEURIN SUPERFAMILY; 1.
DR   PANTHER; PTHR43143:SF5; SECRETED PROTEIN; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF00932; LTD; 2.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR   PROSITE; PS51841; LTD; 2.
PE   4: Predicted;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Reference proteome {ECO:0000313|Proteomes:UP000321574};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1924
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039629678"
FT   TRANSMEM        1897..1918
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          282..415
FT                   /note="LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51841"
FT   DOMAIN          561..701
FT                   /note="LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51841"
FT   DOMAIN          1890..1924
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          41..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1214..1234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1752..1888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..133
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..178
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1214..1225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1752..1773
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1797..1807
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1815..1827
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1829..1851
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1871..1883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1924 AA;  215883 MW;  6F1FD14C3116528D CRC64;
     MKMKKGKVHS FVAAVSATMI FATTLWPGTT VVLAESTYPK GEQPTFEVSK DKKQNQDTKQ
     TKEKTEFHQK NEKKTKQPDM TDENHSLPEE EQDEEPKSDE KQKVTGNEDK SSDSEEKYPN
     EEGDENETDE EGKESETSNS NDEKHDASKE GKTKEHQEDE IEDDLDKDEE TIEEDEELRI
     EHEPITKINK NEELLIEASV PNANKVMIQY QTGKQMQTEN IPLQRKADTD IYQFKLRKEM
     TEHLFWSPVF YYSIHAENEA GEKVSTDVIE VDIVDNKTID YNQIPPLLIT EITPDTANVN
     KKDAYEFIEI YNNTNQPIQM NDYEIIYRYP DGKADFTWKI KDDKTVEPQD TFIVWIHNEG
     NKNLTLEDFN KHYGLQLTDD DVAIVHSDGM ANGSERTILL ADKYQNEISG ATYTKQDVTA
     DKGIVYAYPT SGKMMKKVGI SETITPSEII PGQVPAEPVQ VDAEGEAPVI KHEQPKITDE
     EVIELSVEVT SEEDLLGVKA HVKQSDDAKE KTIQMEETDD PTIFTVRIPR KEIWGDTLYY
     YFTAANQAGE TKSETFELEM PENQVDFQNL PELLITELVP DSSNVNALDG YEFIEVYNNS
     NQDINFSEYV IRYRYPNTDK SGDLLWEPTS DTDVIIPSGE AIVFWIINGG NGHLSGADFN
     QNYGTNLVEG KNLFRMSNNG MANGSERTLI VATKSGHEIA RSAYNTDERE DDTVKDKGIF
     YRYPADGTID SVKFSAGVLD ATPGTVTEAQ VPAEKVQLKE DHEKPVIEDK TGSKEIPSSE
     PVIIEAKITD NERVTSAAIF YRTDETKNFK KVNVEEQKKH RYRLKIYAPE LIGKNQLEYY
     FVASDGTSTV KTEPQQIKIV HDHVLEGLRL NVADGDILSG ERLIKATGDN ATDNVQLFIG
     DKELTDKTKA LETEAYFAFD IRKTNLYFKN GVTMGDDILH IFDDTVNEFT TLTVPVEPER
     LKVGENTISV RSGTKVSPFD LESTENRDDF YLKNIRLVLA DGTVIRDADY PDAGKEYAIG
     DSAGMSSVYD FTFTLEEDQF KANAYLIDTT LLKDGEHEIK AVLDEETVSA NVVVDNTAPI
     INPTINNGET YKGKFTIDAA FTDELSDVTE TNAQLNGDYI SLPFETSSAL LDAGEHKVVF
     TAMDEAGNTR TKTVTFQTKA EHPLLPDASP DEAEATETNL TVKVTDPTGD EMDVSFYEAF
     QYKADSDDMS ISMHASDTEP PQNFTPEGEK KLTDSEREKL IKKDGKAITT ESITQFPYHR
     FDVAVDEKVQ ADDIVEIVWN GSSLAGRKVT MYAWNVKTSK WEALISTIAG EEEFELIGKV
     TAGDYMKDRN ISVIVQDEIA KDRVDDTDGA TDIADSEVSR DSSHPVAEEL QTIKSDDTDN
     SGDYRDVLDL PVKDGQFSFV WFSDTQYYSE SYPHIFENQV NWIVDAAEGL NLKYVFHTGD
     LVDKHYDPKQ WEVADSNMKI LDDANIPYGV LAGNHDVGHK GNDYENYYQY FGEDRYIDRD
     YFGESYLNNR GHYDLISAEG NDFIMVYMGW GVDEDGIDWL NDVLEKYPNR KAVLNFHEYL
     LASGSRSPIG DKIFEEVVVP NENVHAVLGG HYHNSQKLED RIDDDGDGKP DRTVYQMLAN
     YQAGPEGGQG FLRILTFDPE TNTMDMTAYS PYLNEKDYYD PELYPGKDSF VVDWDLTPQE
     KKVETDYIEV NVYTDKLIGK VENVPSGETA TVVWNDLEPN ETYFWYATAE DNYGGKTNSP
     IWSFLTKDGE VIEPEEPGDD AGGDDGDVDP GDDENPKEPG GDNNPGDGGK PGMPEKPGSD
     GKPEVPGKPE VPGKPGSGNQ PGNGNKPGNG EKPENDKNLE KPSKPGKDRT NNDGNGPIIE
     KPKEKDDDSN DNGWLSNNKT NGRNKAGTGL PSTATNMYNY IIAGIALLVL GTATMLLLRR
     RKTN
//
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