ID Q63G96_BACCZ Unreviewed; 1112 AA.
AC Q63G96;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE SubName: Full=Possible internalin protein {ECO:0000313|EMBL:AAU19781.1};
GN OrderedLocusNames=BCE33L0459 {ECO:0000313|EMBL:AAU19781.1};
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU19781.1, ECO:0000313|Proteomes:UP000002612};
RN [1] {ECO:0000313|Proteomes:UP000002612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the internalin family.
CC {ECO:0000256|ARBA:ARBA00009432}.
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DR EMBL; CP000001; AAU19781.1; -; Genomic_DNA.
DR AlphaFoldDB; Q63G96; -.
DR KEGG; bcz:BCE33L0459; -.
DR Proteomes; UP000002612; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd06920; NEAT; 1.
DR Gene3D; 2.60.40.1220; -; 2.
DR Gene3D; 2.60.40.1850; -; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR006635; NEAT_dom.
DR InterPro; IPR037250; NEAT_dom_sf.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR46652; LEUCINE-RICH REPEAT AND IQ DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46652:SF3; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 9 ISOFORM X1; 1.
DR Pfam; PF12799; LRR_4; 2.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF05031; NEAT; 1.
DR SMART; SM00364; LRR_BAC; 4.
DR SMART; SM00365; LRR_SD22; 11.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00725; NEAT; 1.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF158911; NEAT domain-like; 1.
DR PROSITE; PS51450; LRR; 11.
DR PROSITE; PS50978; NEAT; 1.
PE 3: Inferred from homology;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1112
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004266390"
FT TRANSMEM 1088..1105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..157
FT /note="NEAT"
FT /evidence="ECO:0000259|PROSITE:PS50978"
FT REGION 839..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1112 AA; 125367 MW; 3B9BF89B3BCAEFF2 CRC64;
MLVAATLSLP FAVYATPILA ATAATENMAV QSPKKHVFDA VIKAYKDNSD EESYATVYIK
DPKLTIENGK RIITATLKDS DFFDYLKVED SKEPGVFHDV KVLSEDKRKH GTKVIQFEVG
ELGKRYNMQM HILIPTLGYD KEFKIQFEVN MRTFVESDIE EDEEEQIEDT QNIIRDKRLQ
QAINKNVLNR KDVNEPIFEE DLKEIKELNI YAGQGIESLK GLEYMENLER ITIQGSDVRN
IAPISQLKRL KVVDLSFNKI ENVEPLVNLE KLDILELQNN RIADVTPLSQ LKKVRTINLS
GNKISDIKPL YNVSSLRKLY VSNNKITDFT GIEQLNKLGT LGVGSNGLVN IEPISQMSGI
VELNLEKNDI KDITSLSKLT GLQSLNLEEN YVSDVSSLSN LINLYELKLA TNEIRDIRPI
QELGKRIKID AQRQKVFLDE AYMNEEVKIP VYDVNGTALQ NIEWKSEGGS ITNGVIKWNS
LGEKMYEFKM DAGESKIRFQ GRVIQNIVEK REESSNVIQD MKLRQYMNKH NFERKNVNTP
ITKEDLLTVK ALKITDGKKE GITDFSGLEF MTNMEELILQ NANMKNVKFI SSLRNLKSVD
LSYNQIEDIK PLHSLENLEK LNISNNGIKN VPELFKMQTL KTLDLSNNKL DNAALDGIYQ
LENLDALLVN NNEINNLDEI GKVSKLNKLE MMGNKVRDIS PLANLKNLQW LNLANNKIQD
ISSLSSILDL LSLKLAGNEI RDVRPIIQLA QWITVDIKNQ KIVLEDGQMN QEIQIPIYDL
EGEIFEDIEL KSEAGIVTDR GTVVWKTPGE KNYVFSLNGN YHGLSLLFSG TVMQNIVAKE
EPKEPVEEVE GSKEEPIKEA EGSKEEPKGP AKEVEGPKEE VKEPAKEVEG PKEEVKEPAK
EVEGLKEEVK EPAKEVEGPK EEVKEPAKEV EGPKEEVKEP AKEVEGPKEE VKEPAKEVEG
PKEEVREPTK EVEGPKEEVK EPMKEVEGSK EEVKEPTKEA EGSKEEVKEP TTEVEGSKEV
KEPGKEVEGS KDAINQSAVA QETNVNNQVG KEKVVENQNM KENKPAVTKQ EESKKSLGAT
GGQENTSTLL SGLALVLSAL SMFVFRKRLF KK
//