ID Q72XP3_BACC1 Unreviewed; 975 AA.
AC Q72XP3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=LPXTG-motif cell wall anchor domain {ECO:0000313|EMBL:AAS44232.1};
GN OrderedLocusNames=BCE_5332 {ECO:0000313|EMBL:AAS44232.1};
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523 {ECO:0000313|EMBL:AAS44232.1, ECO:0000313|Proteomes:UP000002527};
RN [1] {ECO:0000313|EMBL:AAS44232.1, ECO:0000313|Proteomes:UP000002527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248 {ECO:0000313|Proteomes:UP000002527};
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.,
RA Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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DR EMBL; AE017194; AAS44232.1; -; Genomic_DNA.
DR AlphaFoldDB; Q72XP3; -.
DR KEGG; bca:BCE_5332; -.
DR HOGENOM; CLU_302213_0_0_9; -.
DR Proteomes; UP000002527; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.740; -; 4.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR047589; DUF11_rpt.
DR InterPro; IPR026466; Fim_isopep_form_D2_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001434; OmcB-like_DUF11.
DR InterPro; IPR041033; Prealbumin-like.
DR NCBIfam; TIGR01451; B_ant_repeat; 4.
DR NCBIfam; TIGR04226; RrgB_K2N_iso_D2; 3.
DR PANTHER; PTHR34819:SF3; CELL SURFACE PROTEIN-RELATED; 1.
DR PANTHER; PTHR34819; LARGE CYSTEINE-RICH PERIPLASMIC PROTEIN OMCB; 1.
DR Pfam; PF01345; DUF11; 4.
DR Pfam; PF17802; SpaA; 1.
DR SUPFAM; SSF49401; Bacterial adhesins; 4.
DR SUPFAM; SSF49478; Cna protein B-type domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 951..968
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 290..406
FT /note="DUF11"
FT /evidence="ECO:0000259|Pfam:PF01345"
FT DOMAIN 441..554
FT /note="DUF11"
FT /evidence="ECO:0000259|Pfam:PF01345"
FT DOMAIN 587..693
FT /note="DUF11"
FT /evidence="ECO:0000259|Pfam:PF01345"
FT DOMAIN 723..831
FT /note="DUF11"
FT /evidence="ECO:0000259|Pfam:PF01345"
FT DOMAIN 864..924
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT REGION 55..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 108412 MW; E9CCED183A4EACF5 CRC64;
MNIWRRKKKL RRQKTFLVLL MLLLVFADIP ISFIDNMTMH AETDSITEQP KDIEIGSVKE
QPNPEAVKDF DPGPPYEQNV AKDIPVEVGE ERIGTSSWIK DIAPASLVDN TCVQQNRVVL
KNGGFEKPRI TKDFFIDQDN VEGWRTTDRY KVIEIWRTRD RIPLPSPLPA EGEQFAELNA
REPGMLYQDV KTTPGQTIYW RLAHRGRDGK DTMRVRIGSA SANITSLPTI QTMEDDNKAW
GRYSGTYTVP AGQTLTRFGF EAVKTYGNAL SVGNFLDDIF LGTEPCVTAT KSVSPEGKVY
AGDELTYTVN VKNHGGDVAG EAMFTDMIPD GTEYVPGSIK LKADGTEKAI TDAEDNDAGF
YKDKKVTVKL GDVQNTEEDP NGITVQFKVR ALPSYIGKQV TNKARIDYGN LLKGSKEYTN
SNEVVNEVIA RNPEIESVKE VKNVQGKSRY EVGDTIEYTV KMRNKIENSI AKKIVIEDSL
PNGIDYVPGT IKVDGKAVTD AVDQDSGHYT IGKVMGNLGD ITDTGWHTVT FQAKVKSDQL
DKTIRNIGKI TGENITPQEP EKSIVIEPKD PKLETVKEAK NLQQGKSIYE VGDTIEYTVK
MRNNVASSVI NNAIIEDPLP EGVEYVPGTI RIDGKVVTDA EDGDSGHYKT GKITGKFGDI
RDTEWHTVVF HVKVKTNQAG KEIVNKAKVT GENITPQEPE KLVKVDYKNP KVESVKEVKN
LQQGKKYEVK DTIEYTIKVR NTVKDSIIRN SLVEDQLPEG VEYVPGSIRV DGNIVTDAED
TDSGHYKAGK VIGKLGDIQD TEWHTIVFQV KIKDGYEDKK ILNVGTVKGD NISPQKPSVE
IAVEPPPSGK IEIEKVDAKD HTLKLKNAEF QIIDKDGNVV GKLVTDESGK AISEPLVFGK
YEIKEIKAPT GYMILKESIH VELTSPLQKL KVENNKSEWV IPNTGGFGTN LIYLFSTLLI
VLTLFLYFRK GDSNL
//