ID A0A0K9F4N0_9BACI Unreviewed; 1725 AA.
AC A0A0K9F4N0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Gram-positive cocci surface proteins LPxTG domain-containing protein {ECO:0000259|PROSITE:PS50847};
GN ORFNames=ACZ11_18215 {ECO:0000313|EMBL:KMY29061.1};
OS Lysinibacillus xylanilyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=582475 {ECO:0000313|EMBL:KMY29061.1, ECO:0000313|Proteomes:UP000037326};
RN [1] {ECO:0000313|Proteomes:UP000037326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23493 {ECO:0000313|Proteomes:UP000037326};
RG Consortium for Microbial Forensics and Genomics (microFORGE);
RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA Blagden T., Winegar R.A.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KMY29061.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFXJ01000010; KMY29061.1; -; Genomic_DNA.
DR RefSeq; WP_049667964.1; NZ_LFXJ01000010.1.
DR PATRIC; fig|582475.4.peg.2697; -.
DR Proteomes; UP000037326; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR Gene3D; 2.60.40.740; -; 4.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR008456; Collagen-bd_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR041033; Prealbumin-like.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR Pfam; PF05737; Collagen_bind; 3.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF17802; SpaA; 1.
DR SUPFAM; SSF49401; Bacterial adhesins; 4.
DR SUPFAM; SSF49478; Cna protein B-type domain; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1700..1717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1691..1725
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 37..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1644..1691
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 48..62
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1725 AA; 187668 MW; 151D8B6339DD15E4 CRC64;
MKKLKRLNIA IILMLLVFQT VLSPISVFAD DVSSIPSELK QQADNEKEID IDGEEISDND
SVITEEESTS QTSESDIKED IGEAEEGDNE AEETTNNPAE IVPEPLTAQQ IPAKLTSFEM
KIGGETVRDG SFDTELPQDT LANFTVKFSV PLQNDQEEAW GDGSWFEFQL PKSLIDFDEA
FKGSKSENGI TYTYTTTGNK VRVELNGMEP GSGSSQPAEL IISFNSGFNN LSDEREQELE
IPSITGGSET IKAEFTFLPS TSKKEVSKSA VGTPTPTASG NHEMEWQVWV NEAGKTLSNP
TLKDIATSSA GSPSHEIVDN SVNVYQYEVG LSGVKNKNGD GDHVLTDGNW GDINSTLTGK
YAYKITYKTA VSLDDNKRDG AVNFNNQVEF INDGQSNETS KATHTITYGK ALDKKLVSNT
NYQTKWRIDY NHNLLNISQA KLTDTITGPH EIDASSIKVY KMNDATGNVV NQVSQGEEIT
KGFEISPNTG NVKTFTLTFD SAISDAYTIV YDANYNKQDF YETVTGPFNN SVTSDSGKTE
NETYQLVENL LNKSHKVDFD NKVITWTINI KSDNPNKPIN NLTLTDTFTA DSADGAHELI
ANSVKLNGKN ATYTLIDGDK KKGFTIKDIN VDPGQTATII YQTSFAIDDN GVVQNQGYGN
TAATHWISGG KTYDKTVTDK YVPDTTTVNN GSKSGKFDYV TQELTWDVKV NINKKNINGA
VLVDTVGDGH KYVPETIEVL PLTNLGGSDT GGTIGTTPIS SDYYVVSDES DKGFTLTFID
SLPEEINNQA YVVRYKTMDD DKILGVGSGN ASEKGNVYTN GATFKTKGTK EFTLDSTPVT
IDENVANNLI TKNTPTQNAA KELITWTLDV NKSHSDLGKD VTLTDLPGNN LMLLEDSIKI
APYTVTPTGI KNGDWQTPAQ LGLSVTFDKV GGFSIVFPDL IKKGYRVKYE TVGFGKINDS
LVNTATLNYT GQTMANQQTE DEFNGKFSFS SSESSFTSTR GSAKFKKVGI DTATGQIKEN
LAGVTFQLIK RTATPNEYII KTATTDANGE FTFDNVPYND YLIREVAAPT GYDKMKDYPF
KLNGDTTLDS KPDLVTQLVN TTTVIGRACT QFEITINDID GESITTGTVT LIDKNGVETA
PYKVTNGKVK LPKNFTAGEY TVIHSVEGNL GKVTVKYGVV CKDTIQPAPK CDNFTIVVED
TEGIRTNIKD LTLKSGTTEV KASPDASGKF IFESNKNNPT NGVKPGEYMV YEGKQFLGTV
NLTYTKDCGH EFIVKQLPKC EEFELTVKDV DGNKITDSTT TIVVKDVNGK EIINTTTTTG
VIKLTNLEPD TYTVEVNSEK IGTFQTNSEC EATVQPAPKC DLFTLTVKDE NGNPRPNVSN
ITIKDKTTGA IIATNKTTNE LGQITINPKE IPSGDYSVYQ GDLFIGKITV KYSERCNAEI
SAAPACPSFT LTVLTQFGTP NANAKITIKD AKGNSVKGAD DNEVLTTSIA GTVVLPNEAI
KQGTYNVYEG SSLIGSFTVK DTCSATVQPS TGGGGGKPDP EKPVDPEKPK PEPEKPVDPN
KPKPEPEKPV KPKPEKPVDP NKPNPDPEKP VNPNKPNPGN PTTDTKNPTS PGKPETTKPS
VEEVIDQGKE LKPYNPSTAD KDTLDAHKDL LDKYNKLSKE EQAEVDKYLD IDKIKADAKE
MEAQLNAQGK LPQTNGANQT ALTLIGVALV LGALFLLRRR NEEVK
//