ID K8EVB1_CARML Unreviewed; 1713 AA.
AC K8EVB1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=LPXTG-motif cell wall anchor domain protein {ECO:0000313|EMBL:CCO12616.2};
GN ORFNames=BN424_3195 {ECO:0000313|EMBL:CCO12616.2};
OS Carnobacterium maltaromaticum LMA28.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO12616.2, ECO:0000313|Proteomes:UP000000212};
RN [1] {ECO:0000313|Proteomes:UP000000212}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., Afzal M.I.,
RA Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL Genome Announc. 1:0-0(2013).
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000256|ARBA:ARBA00007257}.
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DR EMBL; HE999757; CCO12616.2; -; Genomic_DNA.
DR RefSeq; WP_015077607.1; NC_019425.2.
DR STRING; 1234679.BN424_3195; -.
DR KEGG; cml:BN424_3195; -.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_000297_3_1_9; -.
DR OrthoDB; 2158979at2; -.
DR Proteomes; UP000000212; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.740; -; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR041033; Prealbumin-like.
DR InterPro; IPR041171; SDR_Ig.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR36108:SF13; COLOSSIN-B; 1.
DR PANTHER; PTHR36108; COLOSSIN-B-RELATED; 1.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF17802; SpaA; 7.
DR SUPFAM; SSF49401; Bacterial adhesins; 5.
DR SUPFAM; SSF49478; Cna protein B-type domain; 7.
PE 3: Inferred from homology;
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:UP000000212};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1713
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038573152"
FT TRANSMEM 1685..1704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 148..208
FT /note="SDR-like Ig"
FT /evidence="ECO:0000259|Pfam:PF17961"
FT DOMAIN 1020..1078
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1114..1180
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1207..1274
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1299..1366
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1392..1460
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1486..1552
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1579..1644
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1673..1710
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|Pfam:PF00746"
FT REGION 32..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1713 AA; 187604 MW; EC3E64C01BADF9D8 CRC64;
MKNKIITLFL VTMLVFQVSS PALIYAEGTA TETNSSQHDA EIPATAESSL PTGIAPVEEP
TTQVENEENS TEVDTPTKPE EVPTSTQAEE NQPVESNEVK PETTNKQPET LIEKAPKLAI
TDNLFTNIKM YKINGDEVKE NDIIPNMSGI KLNMTFSFTN KNYQTGDTFT TQLPPQIAIA
KDLSGDFSPM TSAKWAINAA TKKLTITFLE DNIASEEYKL SLITSLEKVS NSAEENQEII
FTTTPNETIY HLEVTSNIDS GKSSTAITVG DFNPKTAKIE SIFNLDRTDS ANRRFTVEPY
QSDSKLVFDS VKVSTSDVDF NGVLVGEKTE LTEGVDFQVT KKNSGTYQAT AEIKLTNKLN
KKAIIVESSL SGINGKSYID DSTSGNEYNY FYSYSYTYED GKNSQYSFAS QNFYTVQPLT
TSGKINKETG FIDWTIDYNF NEQPLTTMSK LTTDLANQGV EYIPDSLKIE KIGFNYISGN
NYTVIEQGDG ADQWGTPSIN TNGTIQMNAN GATNQAYRVT YSTKITDPTE RVITNKISDG
TTQKEAKISL IPNLLQKESG KIDVFNQTME WSITINAEKY TMKNPVIHDY FIDSVVSHTS
LTVKKKLSET QFENLTEGID YKVTLFDETG SPVGAQPNVN GAPASFNGGV RIDLLGEYAQ
LKDTLVVTIN TKLNTSEEET EIKNKATLNY GDVPGVIEYE AKGTFIDPYY TGGQKMGEAA
VSDGQYLYQN WLILVNSKGS NFNQTSLSDT LPLGSELVPG SLRFEEVTSQ SMLDNMRNYL
RYDYNLVPVG DDVYPTKIDT ENNALNLEFN KLGSKRVYVK YKTRVKKDWY TYNQLKNKAV
VKYDTKTAEY ETTVYAYNYE MALTKAVTLD SAKENVANWT VTTKSISTNL PVENPVISDT
LDNGSTNAAY DPISFVVKNT ATGEKISSDH YSLKITGNTF TITFTDYKAE SNIQVTYNTI
SEFPGGVKSK AQVDSASYVG LNAYYRQAEA AINLGFSSGS GSGIVKTADL TILKVDNLDE
STLLAGATFE ILKADGTETG LKGDTDAQGE LTFTGLPLGD YQLKETKAPT GYDINPEYKT
GKLISLTESM LPIKVTNERT FLNSVTLKKT AKESNESLAG AVFELQDETG TPLESALTTD
VNGTLTLQDL KVGSYQFVET KAPTGYKLDE TPLTFEIKKG QTESVEVAMT NELLPGGVVL
TKTDEQSGET LQGAVFELQK NNKEVIQSGL TTDNLGKLAV DELKPGSYQF VETKAPTGYE
LDTTPVEFTI AKNQSEATEV TMTNKLTPSG IVITKTDDQT GEVLAGAVFE LQDSEGKQVQ
STLTTDESGK ISVNDLAPNA YQLVETKAPV GYQLDATPVP FKIGKGQTEA LKIAITNKAN
PSSVLLTKVD SQTGTVLQGA IFELQDQSGK VLQRDLVTNA SGKLAVSGLK PGSYQFVETK
APTGYQLNQE PVVFTLEKDQ TEAVNITVSN ELIAGVVVLT KIDERSGETL AGAEFDLQDS
QGNKLIQHMV TDAAGKLAIN DLKANDYQLV ETKAPAGYQL DQEPVIFTVE KGQSSALQLS
KTNKAKQQTV RVQKKDAKTD ELLAGAIFDL QDKDGKVIQK NLETGENGTL EISDLANGDY
QLVETKAPTG YKLEQTPMNF SIAQGSDLIT VDKYNDQLNN KTLPRTSVSK NNTYTLPKTG
ENPSVKWMVI GSLVVMTAML AYIVQRRKGE LLK
//
